A potential food biopreservative, CecXJ-37N, non-covalently intercalates into the nucleotides of bacterial genomic DNA beyond membrane attack

•CecXJ-37N shows small MICs (0.25–7.8μM) against 8 food-borne pathogenic strains.•CecXJ-37N shows low hemolysis and no cytotoxicity to normal mammalian cells.•CecXJ-37N induces pore-forming on E. coli cell membrane and causes cytolysis.•CecXJ-37N penetrates bacterial cell membrane and interacts with...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Food chemistry Jg. 217; S. 576 - 584
Hauptverfasser:	Liu, Dongliang, Liu, Jun, Li, Jinyao, Xia, Lijie, Yang, Jianhua, Sun, Surong, Ma, Ji, Zhang, Fuchun
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	England Elsevier Ltd 15.02.2017
Schlagworte:	Amide modification Animals Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - pharmacology antibacterial properties Antimicrobial Cationic Peptides - chemistry Antimicrobial Cationic Peptides - pharmacology Antimicrobial peptide Cell Membrane - drug effects Cell membrane penetration Cell Survival - drug effects cytoplasm cytotoxicity DNA DNA intercalation DNA, Bacterial - chemistry Escherichia coli Escherichia coli - drug effects flow cytometry fluorescence microscopy food biopreservatives Food Contamination - prevention & control food industry Food Microbiology Food preservative Food Preservatives - chemistry Food Preservatives - pharmacology Food-borne pathogen genome Genome, Bacterial hydrolysis mechanism of action Mice Microbial Sensitivity Tests Molecular Structure NIH 3T3 Cells novel foods nucleotides pepsin scanning electron microscopy trypsin ultraviolet-visible spectroscopy Food preservative Cell membrane penetration Food-borne pathogen Amide modification DNA intercalation Antimicrobial peptide
ISSN:	0308-8146, 1873-7072, 1873-7072
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Abstract	•CecXJ-37N shows small MICs (0.25–7.8μM) against 8 food-borne pathogenic strains.•CecXJ-37N shows low hemolysis and no cytotoxicity to normal mammalian cells.•CecXJ-37N induces pore-forming on E. coli cell membrane and causes cytolysis.•CecXJ-37N penetrates bacterial cell membrane and interacts with genomic DNA.•CecXJ-37N intercalates into nucleotides rather than binds to DNA backbone. The antibacterial activities and mechanism of an amide-modified peptide CecXJ-37N were investigated in this study. CecXJ-37N showed small MICs (0.25–7.8μM) against eight harmful strains common in food industry. The α-helix proportion of CecXJ-37N increased by 11-fold in prokaryotic membrane comparable environments; cytotoxicity studies demonstrated the MHC was significantly higher than that of non-amidated isoform. Moreover, CecXJ-37N possessed stronger capacities to resist trypsin and pepsin hydrolysis within two hours. Flow cytometry and scanning electron microscopy demonstrated that CecXJ-37N induced pore-formation, morphological changes, and lysed E. coli cells. Fluorescence microscopy indicated that CecXJ-37N penetrated E. coli membrane and accumulated in cytoplasm. Further ultraviolet–visible spectroscopy suggested that CecXJ-37N changed the action mode of parental peptide interacting with bacterial genome from outside binding to a tightly non-covalent intercalation into nucleotides. Overall, this study suggested that amide-modification enhanced antimicrobial activity and reduced the cytotoxicity, thus could be potential strategies for developing novel food preservatives.
AbstractList	The antibacterial activities and mechanism of an amide-modified peptide CecXJ-37N were investigated in this study. CecXJ-37N showed small MICs (0.25-7.8μM) against eight harmful strains common in food industry. The α-helix proportion of CecXJ-37N increased by 11-fold in prokaryotic membrane comparable environments; cytotoxicity studies demonstrated the MHC was significantly higher than that of non-amidated isoform. Moreover, CecXJ-37N possessed stronger capacities to resist trypsin and pepsin hydrolysis within two hours. Flow cytometry and scanning electron microscopy demonstrated that CecXJ-37N induced pore-formation, morphological changes, and lysed E. coli cells. Fluorescence microscopy indicated that CecXJ-37N penetrated E. coli membrane and accumulated in cytoplasm. Further ultraviolet-visible spectroscopy suggested that CecXJ-37N changed the action mode of parental peptide interacting with bacterial genome from outside binding to a tightly non-covalent intercalation into nucleotides. Overall, this study suggested that amide-modification enhanced antimicrobial activity and reduced the cytotoxicity, thus could be potential strategies for developing novel food preservatives.The antibacterial activities and mechanism of an amide-modified peptide CecXJ-37N were investigated in this study. CecXJ-37N showed small MICs (0.25-7.8μM) against eight harmful strains common in food industry. The α-helix proportion of CecXJ-37N increased by 11-fold in prokaryotic membrane comparable environments; cytotoxicity studies demonstrated the MHC was significantly higher than that of non-amidated isoform. Moreover, CecXJ-37N possessed stronger capacities to resist trypsin and pepsin hydrolysis within two hours. Flow cytometry and scanning electron microscopy demonstrated that CecXJ-37N induced pore-formation, morphological changes, and lysed E. coli cells. Fluorescence microscopy indicated that CecXJ-37N penetrated E. coli membrane and accumulated in cytoplasm. Further ultraviolet-visible spectroscopy suggested that CecXJ-37N changed the action mode of parental peptide interacting with bacterial genome from outside binding to a tightly non-covalent intercalation into nucleotides. Overall, this study suggested that amide-modification enhanced antimicrobial activity and reduced the cytotoxicity, thus could be potential strategies for developing novel food preservatives. The antibacterial activities and mechanism of an amide-modified peptide CecXJ-37N were investigated in this study. CecXJ-37N showed small MICs (0.25–7.8μM) against eight harmful strains common in food industry. The α-helix proportion of CecXJ-37N increased by 11-fold in prokaryotic membrane comparable environments; cytotoxicity studies demonstrated the MHC was significantly higher than that of non-amidated isoform. Moreover, CecXJ-37N possessed stronger capacities to resist trypsin and pepsin hydrolysis within two hours. Flow cytometry and scanning electron microscopy demonstrated that CecXJ-37N induced pore-formation, morphological changes, and lysed E. coli cells. Fluorescence microscopy indicated that CecXJ-37N penetrated E. coli membrane and accumulated in cytoplasm. Further ultraviolet–visible spectroscopy suggested that CecXJ-37N changed the action mode of parental peptide interacting with bacterial genome from outside binding to a tightly non-covalent intercalation into nucleotides. Overall, this study suggested that amide-modification enhanced antimicrobial activity and reduced the cytotoxicity, thus could be potential strategies for developing novel food preservatives. •CecXJ-37N shows small MICs (0.25–7.8μM) against 8 food-borne pathogenic strains.•CecXJ-37N shows low hemolysis and no cytotoxicity to normal mammalian cells.•CecXJ-37N induces pore-forming on E. coli cell membrane and causes cytolysis.•CecXJ-37N penetrates bacterial cell membrane and interacts with genomic DNA.•CecXJ-37N intercalates into nucleotides rather than binds to DNA backbone. The antibacterial activities and mechanism of an amide-modified peptide CecXJ-37N were investigated in this study. CecXJ-37N showed small MICs (0.25–7.8μM) against eight harmful strains common in food industry. The α-helix proportion of CecXJ-37N increased by 11-fold in prokaryotic membrane comparable environments; cytotoxicity studies demonstrated the MHC was significantly higher than that of non-amidated isoform. Moreover, CecXJ-37N possessed stronger capacities to resist trypsin and pepsin hydrolysis within two hours. Flow cytometry and scanning electron microscopy demonstrated that CecXJ-37N induced pore-formation, morphological changes, and lysed E. coli cells. Fluorescence microscopy indicated that CecXJ-37N penetrated E. coli membrane and accumulated in cytoplasm. Further ultraviolet–visible spectroscopy suggested that CecXJ-37N changed the action mode of parental peptide interacting with bacterial genome from outside binding to a tightly non-covalent intercalation into nucleotides. Overall, this study suggested that amide-modification enhanced antimicrobial activity and reduced the cytotoxicity, thus could be potential strategies for developing novel food preservatives.
Author	Li, Jinyao Zhang, Fuchun Ma, Ji Yang, Jianhua Sun, Surong Xia, Lijie Liu, Dongliang Liu, Jun
Author_xml	– sequence: 1 givenname: Dongliang surname: Liu fullname: Liu, Dongliang organization: Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, 830046 Urumqi, China – sequence: 2 givenname: Jun surname: Liu fullname: Liu, Jun organization: Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, 830046 Urumqi, China – sequence: 3 givenname: Jinyao surname: Li fullname: Li, Jinyao organization: Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, 830046 Urumqi, China – sequence: 4 givenname: Lijie surname: Xia fullname: Xia, Lijie organization: Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, 830046 Urumqi, China – sequence: 5 givenname: Jianhua surname: Yang fullname: Yang, Jianhua organization: Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, 830046 Urumqi, China – sequence: 6 givenname: Surong surname: Sun fullname: Sun, Surong organization: Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, 830046 Urumqi, China – sequence: 7 givenname: Ji surname: Ma fullname: Ma, Ji organization: Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, 830046 Urumqi, China – sequence: 8 givenname: Fuchun surname: Zhang fullname: Zhang, Fuchun email: zfcxju@qq.com organization: Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, 830046 Urumqi, China
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/27664674$$D View this record in MEDLINE/PubMed
BookMark	eNqFkc1uEzEUhS1URNPCK1ResugM_pmMPRILokALqCobkNhZtucOdZixg-1EykPwzniUZsMmK-va3zk-OvcKXfjgAaEbSmpKaPtuUw8h9PYJppqVuSZdTTh_gRZUCl4JItgFWhBOZCVp016iq5Q2hJDCylfokom2bVrRLNDfFd6GDD47PeLZEhsXthESxL3Obg-3eA3259eKi8dbXEJUNuz1WATjATufIVo96gxpHgLOT4D9zo4QsuvLZRiw0bZQs_0v8GFyFn98XGEDh-B7PMFkovaAdc7a_n6NXg56TPDm-bxGP-4-fV9_rh6-3X9Zrx4q23CZK8EEh2UvO8uNNWYpgdN2SSXtpWC0MyCh4UNnOBcMiNDlUcuu1b0YqAEq-DV6e_TdxvBnBymrySUL41iihF1S7FgVKZWeQ6lkvFkyyWRBb57RnZmgV9voJh0P6tR2Ad4fARtDShEGZV0uLQefo3ajokTNy1UbdVqumperSKdKkiJv_5Offjgr_HAUQul07yCqZB14C72LYLPqgztn8Q_Gi8M8
CitedBy_id	crossref_primary_10_4142_jvs_2021_22_e59 crossref_primary_10_3390_ijms241814053 crossref_primary_10_3390_life13051161 crossref_primary_10_3390_pharmaceutics16121591 crossref_primary_10_3390_ph14010001 crossref_primary_10_1007_s00018_021_03784_z crossref_primary_10_1186_s12866_017_0957_y crossref_primary_10_3390_ijms20235862 crossref_primary_10_1016_j_abb_2021_109095 crossref_primary_10_1111_jfpp_15061 crossref_primary_10_1016_j_micinf_2017_06_002 crossref_primary_10_1016_j_biochi_2022_03_015 crossref_primary_10_3390_ijms22020691 crossref_primary_10_1007_s11130_024_01240_4 crossref_primary_10_3390_ijms23147812 crossref_primary_10_1007_s00203_023_03714_6
Cites_doi	10.1039/b912944h 10.1021/cb500475y 10.1093/nar/gkv1278 10.1371/journal.pone.0098935 10.1016/j.bbagen.2004.11.006 10.3892/etm.2013.1056 10.1038/415389a 10.1016/j.ijantimicag.2012.02.003 10.1128/AAC.01619-12 10.1074/jbc.M413406200 10.1016/j.biochi.2010.02.023 10.1016/j.chembiol.2014.10.009 10.1016/j.bbamem.2007.06.020 10.1007/s00726-010-0632-1 10.1021/jf900668n 10.1016/S0006-3495(01)75802-X 10.1128/AAC.00477-08 10.1074/mcp.T400003-MCP200 10.1093/abbs/gmu070 10.1371/journal.pone.0131008 10.1073/pnas.0406678101 10.1007/s00018-011-0710-x 10.1016/j.actbio.2013.08.043 10.1016/j.biomaterials.2012.09.032 10.1016/j.copbio.2007.09.006 10.1007/s00726-014-1761-8 10.1016/j.bbamem.2014.08.018 10.3390/molecules190810803 10.1016/j.peptides.2012.08.024 10.1021/ja00190a046 10.1128/AAC.49.8.3208-3216.2005 10.1016/0022-1759(83)90303-4 10.1093/jac/31.1.57 10.1016/j.pep.2013.02.013 10.1016/j.bbamem.2012.09.005 10.1016/S0168-1605(99)00072-0 10.1038/nmeth.2089
ContentType	Journal Article
Copyright	2016 Elsevier Ltd Copyright © 2016 Elsevier Ltd. All rights reserved.
Copyright_xml	– notice: 2016 Elsevier Ltd – notice: Copyright © 2016 Elsevier Ltd. All rights reserved.
DBID	AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 7S9 L.6
DOI	10.1016/j.foodchem.2016.09.033
DatabaseName	CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic AGRICOLA AGRICOLA - Academic
DatabaseTitle	CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic AGRICOLA AGRICOLA - Academic
DatabaseTitleList	MEDLINE - Academic AGRICOLA MEDLINE
Database_xml	– sequence: 1 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: 7X8 name: MEDLINE - Academic url: https://search.proquest.com/medline sourceTypes: Aggregation Database
DeliveryMethod	fulltext_linktorsrc
Discipline	Economics Chemistry Diet & Clinical Nutrition
EISSN	1873-7072
EndPage	584
ExternalDocumentID	27664674 10_1016_j_foodchem_2016_09_033 S0308814616314157
Genre	Journal Article
GroupedDBID	--- --K --M .~1 0R~ 1B1 1RT 1~. 1~5 4.4 457 4G. 5GY 5VS 7-5 71M 8P~ 9JM 9JN AABNK AABVA AACTN AAEDT AAEDW AAIAV AAIKC AAIKJ AAKOC AALRI AAMNW AAOAW AAQFI AARLI AATLK AAXUO ABFNM ABFRF ABGRD ABGSF ABJNI ABMAC ABUDA ABYKQ ACDAQ ACGFO ACGFS ACIUM ACRLP ADBBV ADECG ADEZE ADQTV ADUVX AEBSH AEFWE AEHWI AEKER AENEX AEQOU AFKWA AFTJW AFXIZ AFZHZ AGUBO AGYEJ AHHHB AIEXJ AIKHN AITUG AJBFU AJOXV AJSZI ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ AXJTR BKOJK BLXMC CBWCG CS3 DOVZS DU5 EBS EFJIC EFLBG EJD EO8 EO9 EP2 EP3 F5P FDB FIRID FLBIZ FNPLU FYGXN G-Q GBLVA IHE J1W K-O KOM KZ1 LW9 M41 MO0 N9A O-L O9- OAUVE OZT P-8 P-9 P2P PC. Q38 RIG ROL RPZ SAB SCC SDF SDG SDP SES SPC SPCBC SSA SSK SSU SSZ T5K WH7 ~G- ~KM 29H 53G 9DU AAHBH AALCJ AAQXK AATTM AAXKI AAYJJ AAYWO AAYXX ABWVN ABXDB ACLOT ACNNM ACRPL ACVFH ADCNI ADMUD ADNMO AEIPS AEUPX AFJKZ AFPUW AGHFR AGQPQ AGRDE AI. AIGII AIIUN AKBMS AKRWK AKYEP ANKPU APXCP ASPBG AVWKF AZFZN CITATION EFKBS FEDTE FGOYB G-2 HLV HVGLF HZ~ R2- SCB SEW VH1 WUQ Y6R ~HD CGR CUY CVF ECM EIF NPM SSH 7X8 7S9 L.6
ID	FETCH-LOGICAL-c438t-7273e5d89c3bcbb58e3165181d87219be8e43f9b3372e07a165a896ad7f1be173
ISICitedReferencesCount	21
ISICitedReferencesURI	http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000384851800074&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
ISSN	0308-8146 1873-7072
IngestDate	Sun Sep 28 11:42:18 EDT 2025 Sat Sep 27 22:06:18 EDT 2025 Thu Apr 03 07:07:18 EDT 2025 Sat Nov 29 06:45:04 EST 2025 Tue Nov 18 21:25:06 EST 2025 Fri Feb 23 02:24:42 EST 2024
IsPeerReviewed	true
IsScholarly	true
Keywords	Food preservative Cell membrane penetration Food-borne pathogen Amide modification DNA intercalation Antimicrobial peptide
Language	English
License	Copyright © 2016 Elsevier Ltd. All rights reserved.
LinkModel	OpenURL
MergedId	FETCHMERGED-LOGICAL-c438t-7273e5d89c3bcbb58e3165181d87219be8e43f9b3372e07a165a896ad7f1be173
Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
PMID	27664674
PQID	1823452828
PQPubID	23479
PageCount	9
ParticipantIDs	proquest_miscellaneous_2000201003 proquest_miscellaneous_1823452828 pubmed_primary_27664674 crossref_citationtrail_10_1016_j_foodchem_2016_09_033 crossref_primary_10_1016_j_foodchem_2016_09_033 elsevier_sciencedirect_doi_10_1016_j_foodchem_2016_09_033
PublicationCentury	2000
PublicationDate	2017-02-15
PublicationDateYYYYMMDD	2017-02-15
PublicationDate_xml	– month: 02 year: 2017 text: 2017-02-15 day: 15
PublicationDecade	2010
PublicationPlace	England
PublicationPlace_xml	– name: England
PublicationTitle	Food chemistry
PublicationTitleAlternate	Food Chem
PublicationYear	2017
Publisher	Elsevier Ltd
Publisher_xml	– name: Elsevier Ltd
References	Xia, Zhang, Liu, Ma, Yang (b0165) 2013; 5 Yeung, Gellatly, Hancock (b0185) 2011; 68 Yang, Harroun, Weiss, Ding, Huang (b0180) 2001; 81 Yan, Wang, Dang, Chen, Xie, Zhang (b0175) 2013; 57 Xia, Wu, Kang, Ma, Yang, Zhang (b0160) 2014; 46 Kacprzyk, Rydengård, Mörgelin, Davoudi, Pasupuleti, Malmsten (b0030) 2007; 1768 Palchaudhuri, Hergenrother (b0090) 2007; 18 Schneider, Rasband, Eliceiri (b0100) 2012; 9 Sharma, Nagaraj (b0105) 2012; 38 Wang, Hanke, Mishra, Lushnikova, Heim, Thomas (b0140) 2014; 9 Zhu, Dong, Wang, Ma, Zhang, Ma (b0200) 2014; 10 Xu, Zhu, Tan, Li, Shan (b0170) 2014; 9 Liu, Xia, Xu, Wang (b0060) 2013; 34 Strömstedt, Pasupuleti, Schmidtchen, Malmsten (b0110) 2009; 53 Tan, Huang, Huang, Chen (b0125) 2014; 19 Xia, Liu, Ma, Sun, Yang, Zhang (b0155) 2013; 90 Chen, Mant, Farmer, Hancock, Vasil, Hodges (b0015) 2005; 280 Olsen, Ong, Mann (b0085) 2004; 3 Nordahl, Rydengård, Nyberg, Nitsche, Mörgelin, Malmsten (b0080) 2004; 101 Li, He, Liu, Sheng, Hu, Chen (b0055) 2005; 1722 Takahashi, Shukla, Prakash, Zhang (b0120) 2010; 92 Mardirossian, Grzela, Giglione, Meinnel, Gennaro, Mergaert (b0065) 2014; 21 Zang, Thomas, Liu, Chen, Ling, Zhou (b0190) 2013; 2 Mosmann (b0075) 1983; 65 Whitea, Kays, Friedrich, Del Bene (b0150) 1993; 31 Kang, Xia, Ma, Zhang (b0040) 2014; 39 Tiwari, Valdramidis, O’Donnell, Muthukumarappan, Bourke, Cullen (b0130) 2009; 57 Kamarajan, Hayami, Matte, Liu, Danciu, Ramamoorthy (b0035) 2015; 10 Menousek, Mishra, Hanke, Heim, Kielian, Wang (b0070) 2012; 39 Deslouches, Islam, Craigo, Paranjape, Montelaro, Mietzner (b0020) 2005; 49 Wang, Li, Wang (b0145) 2016; 44 Beevers, Dixon (b0005) 2010; 39 Brul, Coote (b0010) 1999; 50 Kim, Park, Yoon, Hahm, Park (b0045) 2011; 40 Lee, Park, Hahm, Park (b0050) 2013; 1828 Sun, Xia, Li, Du, Liang (b0115) 2014; 1838 Ulvatne, Samuelsen, Haukland, Krämer, Vorland (b0135) 2004; 237 Dong, Zhu, Lv, Ma, Jiang, Shan (b0025) 2014; 46 Zasloff (b0195) 2002; 415 Pyle, Rehmann, Meshoyrer, Kumar, Turro, Barton (b0095) 1989; 111 Kang (10.1016/j.foodchem.2016.09.033_b0040) 2014; 39 Sharma (10.1016/j.foodchem.2016.09.033_b0105) 2012; 38 Zang (10.1016/j.foodchem.2016.09.033_b0190) 2013; 2 Palchaudhuri (10.1016/j.foodchem.2016.09.033_b0090) 2007; 18 Schneider (10.1016/j.foodchem.2016.09.033_b0100) 2012; 9 Whitea (10.1016/j.foodchem.2016.09.033_b0150) 1993; 31 Kacprzyk (10.1016/j.foodchem.2016.09.033_b0030) 2007; 1768 Kamarajan (10.1016/j.foodchem.2016.09.033_b0035) 2015; 10 Tiwari (10.1016/j.foodchem.2016.09.033_b0130) 2009; 57 Nordahl (10.1016/j.foodchem.2016.09.033_b0080) 2004; 101 Strömstedt (10.1016/j.foodchem.2016.09.033_b0110) 2009; 53 Lee (10.1016/j.foodchem.2016.09.033_b0050) 2013; 1828 Pyle (10.1016/j.foodchem.2016.09.033_b0095) 1989; 111 Li (10.1016/j.foodchem.2016.09.033_b0055) 2005; 1722 Menousek (10.1016/j.foodchem.2016.09.033_b0070) 2012; 39 Yeung (10.1016/j.foodchem.2016.09.033_b0185) 2011; 68 Zhu (10.1016/j.foodchem.2016.09.033_b0200) 2014; 10 Beevers (10.1016/j.foodchem.2016.09.033_b0005) 2010; 39 Ulvatne (10.1016/j.foodchem.2016.09.033_b0135) 2004; 237 Xia (10.1016/j.foodchem.2016.09.033_b0165) 2013; 5 Mardirossian (10.1016/j.foodchem.2016.09.033_b0065) 2014; 21 Deslouches (10.1016/j.foodchem.2016.09.033_b0020) 2005; 49 Yan (10.1016/j.foodchem.2016.09.033_b0175) 2013; 57 Wang (10.1016/j.foodchem.2016.09.033_b0145) 2016; 44 Olsen (10.1016/j.foodchem.2016.09.033_b0085) 2004; 3 Xia (10.1016/j.foodchem.2016.09.033_b0155) 2013; 90 Zasloff (10.1016/j.foodchem.2016.09.033_b0195) 2002; 415 Xu (10.1016/j.foodchem.2016.09.033_b0170) 2014; 9 Brul (10.1016/j.foodchem.2016.09.033_b0010) 1999; 50 Tan (10.1016/j.foodchem.2016.09.033_b0125) 2014; 19 Chen (10.1016/j.foodchem.2016.09.033_b0015) 2005; 280 Wang (10.1016/j.foodchem.2016.09.033_b0140) 2014; 9 Dong (10.1016/j.foodchem.2016.09.033_b0025) 2014; 46 Liu (10.1016/j.foodchem.2016.09.033_b0060) 2013; 34 Xia (10.1016/j.foodchem.2016.09.033_b0160) 2014; 46 Sun (10.1016/j.foodchem.2016.09.033_b0115) 2014; 1838 Takahashi (10.1016/j.foodchem.2016.09.033_b0120) 2010; 92 Mosmann (10.1016/j.foodchem.2016.09.033_b0075) 1983; 65 Yang (10.1016/j.foodchem.2016.09.033_b0180) 2001; 81 Kim (10.1016/j.foodchem.2016.09.033_b0045) 2011; 40
References_xml	– volume: 237 start-page: 377 year: 2004 end-page: 384 ident: b0135 article-title: Lactoferricin B inhibits bacterial macromolecular synthesis in publication-title: FEMS Microbiology Letters – volume: 19 start-page: 10803 year: 2014 end-page: 10817 ident: b0125 article-title: Effects of single amino acid substitution on the biophysical properties and biological activities of an amphipathic α-helical antibacterial peptide against Gram-negative bacteria publication-title: Molecules – volume: 39 start-page: 402 year: 2012 end-page: 406 ident: b0070 article-title: Database screening and publication-title: International Journal of Antimicrobial Agents – volume: 101 start-page: 16879 year: 2004 end-page: 16884 ident: b0080 article-title: Activation of the complement system generates antibacterial peptides publication-title: Proceedings of the National Academy of Sciences of the United States of America – volume: 31 start-page: 57 year: 1993 end-page: 64 ident: b0150 article-title: Impact of different statistical methodologies on the evaluation of the in-vitro MICs for bacteroides fragilis of selected cephalosporins and cephamycins publication-title: Journal of Antimicrobial Chemotherapy – volume: 49 start-page: 3208 year: 2005 end-page: 3216 ident: b0020 article-title: Activity of the de novo engineered antimicrobial peptide WLBU2 against publication-title: Antimicrobial Agents and Chemotherapy – volume: 40 start-page: 183 year: 2011 end-page: 195 ident: b0045 article-title: C-terminal amidation of PMAP-23: Translocation to the inner membrane of Gram-negative bacteria publication-title: Amino Acids – volume: 10 start-page: e0131008 year: 2015 ident: b0035 article-title: Nisin ZP, a bacteriocin and food preservative, inhibits head and neck cancer tumorigenesis and prolongs survival publication-title: PLoS ONE – volume: 1828 start-page: 443 year: 2013 end-page: 454 ident: b0050 article-title: Antimicrobial HPA3NT3 peptide analogs: Placement of aromatic rings and positive charges are key determinants for cell selectivity and mechanism of action publication-title: Biochimica et Biophysica Acta (BBA)-Biomembranes – volume: 10 start-page: 244 year: 2014 end-page: 257 ident: b0200 article-title: Design of imperfectly amphipathic α-helical antimicrobial peptides with enhanced cell selectivity publication-title: Acta Biomaterialia – volume: 18 start-page: 497 year: 2007 end-page: 503 ident: b0090 article-title: DNA as a target for anticancer compounds: methods to determine the mode of binding and the mechanism of action publication-title: Current Opinion in Biotechnology – volume: 9 start-page: e98935 year: 2014 ident: b0170 article-title: Design of embedded-hybrid antimicrobial peptides with enhanced cell selectivity and anti-biofilm activity publication-title: PLoS ONE – volume: 111 start-page: 3051 year: 1989 end-page: 3058 ident: b0095 article-title: Mixed-ligand complexes of ruthenium (II): Factors governing binding to DNA publication-title: Journal of the American Chemical Society – volume: 1722 start-page: 15 year: 2005 end-page: 21 ident: b0055 article-title: Binding of the bioactive component jatrorrhizine to human serum albumin publication-title: Biochimica et Biophysica Acta (BBA)-General Subjects – volume: 39 start-page: 2146 year: 2010 end-page: 2157 ident: b0005 article-title: Helical membrane peptides to modulate cell function publication-title: Chemical Society Reviews – volume: 65 start-page: 55 year: 1983 end-page: 63 ident: b0075 article-title: Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays publication-title: Journal of Immunological Methods – volume: 21 start-page: 1639 year: 2014 end-page: 1647 ident: b0065 article-title: The host antimicrobial peptide Bac 7 1–35 binds to bacterial ribosomal proteins and inhibits protein synthesis publication-title: Chemistry & Biology – volume: 280 start-page: 12316 year: 2005 end-page: 12329 ident: b0015 article-title: Rational design of α-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index publication-title: Journal Biological Chemistry – volume: 9 start-page: 1997 year: 2014 end-page: 2002 ident: b0140 article-title: Transformation of human cathelicidin LL-37 into selective, stable, and potent antimicrobial compounds publication-title: ACS Chemical Biology – volume: 39 start-page: 247 year: 2014 end-page: 251 ident: b0040 article-title: Preservation effects of CecropinXJ proteins in fresh squeezed juice publication-title: Food Science and Technology – volume: 9 start-page: 671 year: 2012 end-page: 675 ident: b0100 article-title: NIH Image to ImageJ: 25 years of image analysis publication-title: Nature Methods – volume: 50 start-page: 1 year: 1999 end-page: 17 ident: b0010 article-title: Preservative agents in foods: Mode of action and microbial resistance mechanisms publication-title: International Journal of Food Microbiology – volume: 1838 start-page: 2985 year: 2014 end-page: 2993 ident: b0115 article-title: Relationship between peptide structure and antimicrobial activity as studied by de novo designed peptides publication-title: Biochimica et Biophysica Acta (BBA)-Biomembranes – volume: 2 start-page: 112 year: 2013 ident: b0190 article-title: Preventing breast cancer growth by cationic cecropin B publication-title: Biological System – volume: 53 start-page: 593 year: 2009 end-page: 602 ident: b0110 article-title: Evaluation of strategies for improving proteolytic resistance of antimicrobial peptides by using variants of EFK17, an internal segment of LL-37 publication-title: Antimicrobial Agents and Chemotherapy – volume: 5 start-page: 1745 year: 2013 end-page: 1751 ident: b0165 article-title: Expression and characterization of cecropinXJ, a bioactive antimicrobial peptide from publication-title: Experimental and Therapeutic Medicine – volume: 57 start-page: 220 year: 2013 end-page: 228 ident: b0175 article-title: Two hits are better than one: Membrane-active and DNA binding-related double-action mechanism of NK-18, a novel antimicrobial peptide derived from mammalian NK-lysin publication-title: Antimicrobial Agents and Chemotherapy – volume: 34 start-page: 237 year: 2013 end-page: 250 ident: b0060 article-title: Design of hybrid β-hairpin peptides with enhanced cell specificity and potent anti-inflammatory activity publication-title: Biomaterials – volume: 415 start-page: 389 year: 2002 end-page: 395 ident: b0195 article-title: Antimicrobial peptides of multicellular organisms publication-title: Nature – volume: 38 start-page: 255 year: 2012 end-page: 265 ident: b0105 article-title: Antimicrobial activity of human β-defensin 4 analogs: Insights into the role of disulfide linkages in modulating activity publication-title: Peptides – volume: 57 start-page: 5987 year: 2009 end-page: 6000 ident: b0130 article-title: Application of natural antimicrobials for food preservation publication-title: Journal of Agricultural and Food Chemistry – volume: 92 start-page: 1236 year: 2010 end-page: 1241 ident: b0120 article-title: Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity publication-title: Biochimie – volume: 44 start-page: D1087 year: 2016 end-page: D1093 ident: b0145 article-title: APD3: The antimicrobial peptide database as a tool for research and education publication-title: Nucleic Acids Research – volume: 1768 start-page: 2667 year: 2007 end-page: 2680 ident: b0030 article-title: Antimicrobial activity of histidine-rich peptides is dependent on acidic conditions publication-title: Biochimica et Biophysica Acta (BBA)-Biomembranes – volume: 3 start-page: 608 year: 2004 end-page: 614 ident: b0085 article-title: Trypsin cleaves exclusively C-terminal to arginine and lysine residues publication-title: Molecular & Cellular Proteomics – volume: 81 start-page: 1475 year: 2001 end-page: 1485 ident: b0180 article-title: Barrel-stave model or toroidal model? A case study on melittin pores publication-title: Biophysical Journal – volume: 90 start-page: 47 year: 2013 end-page: 54 ident: b0155 article-title: Expression, purification and characterization of cecropin antibacterial peptide from Bombyx mori in publication-title: Protein Expression and Purification – volume: 46 start-page: 867 year: 2014 end-page: 876 ident: b0160 article-title: CecropinXJ, a silkworm antimicrobial peptide, induces cytoskeleton disruption in esophageal carcinoma cells publication-title: Acta Biochimica et Biophysica Sinica – volume: 68 start-page: 2161 year: 2011 end-page: 2176 ident: b0185 article-title: Multifunctional cationic host defence peptides and their clinical applications publication-title: Cellular and Molecular Life Sciences – volume: 46 start-page: 2137 year: 2014 end-page: 2154 ident: b0025 article-title: Cell specificity and molecular mechanism of antibacterial and antitumor activities of carboxyl-terminal RWL-tagged antimicrobial peptides publication-title: Amino Acids – volume: 39 start-page: 2146 year: 2010 ident: 10.1016/j.foodchem.2016.09.033_b0005 article-title: Helical membrane peptides to modulate cell function publication-title: Chemical Society Reviews doi: 10.1039/b912944h – volume: 39 start-page: 247 year: 2014 ident: 10.1016/j.foodchem.2016.09.033_b0040 article-title: Preservation effects of CecropinXJ proteins in fresh squeezed juice publication-title: Food Science and Technology – volume: 9 start-page: 1997 year: 2014 ident: 10.1016/j.foodchem.2016.09.033_b0140 article-title: Transformation of human cathelicidin LL-37 into selective, stable, and potent antimicrobial compounds publication-title: ACS Chemical Biology doi: 10.1021/cb500475y – volume: 44 start-page: D1087 year: 2016 ident: 10.1016/j.foodchem.2016.09.033_b0145 article-title: APD3: The antimicrobial peptide database as a tool for research and education publication-title: Nucleic Acids Research doi: 10.1093/nar/gkv1278 – volume: 9 start-page: e98935 year: 2014 ident: 10.1016/j.foodchem.2016.09.033_b0170 article-title: Design of embedded-hybrid antimicrobial peptides with enhanced cell selectivity and anti-biofilm activity publication-title: PLoS ONE doi: 10.1371/journal.pone.0098935 – volume: 1722 start-page: 15 year: 2005 ident: 10.1016/j.foodchem.2016.09.033_b0055 article-title: Binding of the bioactive component jatrorrhizine to human serum albumin publication-title: Biochimica et Biophysica Acta (BBA)-General Subjects doi: 10.1016/j.bbagen.2004.11.006 – volume: 5 start-page: 1745 year: 2013 ident: 10.1016/j.foodchem.2016.09.033_b0165 article-title: Expression and characterization of cecropinXJ, a bioactive antimicrobial peptide from Bombyx mori (Bombycidae, Lepidoptera) in Escherichia coli publication-title: Experimental and Therapeutic Medicine doi: 10.3892/etm.2013.1056 – volume: 415 start-page: 389 year: 2002 ident: 10.1016/j.foodchem.2016.09.033_b0195 article-title: Antimicrobial peptides of multicellular organisms publication-title: Nature doi: 10.1038/415389a – volume: 39 start-page: 402 year: 2012 ident: 10.1016/j.foodchem.2016.09.033_b0070 article-title: Database screening and in vivo efficacy of antimicrobial peptides against methicillin-resistant Staphylococcus aureus USA300 publication-title: International Journal of Antimicrobial Agents doi: 10.1016/j.ijantimicag.2012.02.003 – volume: 57 start-page: 220 year: 2013 ident: 10.1016/j.foodchem.2016.09.033_b0175 article-title: Two hits are better than one: Membrane-active and DNA binding-related double-action mechanism of NK-18, a novel antimicrobial peptide derived from mammalian NK-lysin publication-title: Antimicrobial Agents and Chemotherapy doi: 10.1128/AAC.01619-12 – volume: 280 start-page: 12316 year: 2005 ident: 10.1016/j.foodchem.2016.09.033_b0015 article-title: Rational design of α-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index publication-title: Journal Biological Chemistry doi: 10.1074/jbc.M413406200 – volume: 92 start-page: 1236 year: 2010 ident: 10.1016/j.foodchem.2016.09.033_b0120 article-title: Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity publication-title: Biochimie doi: 10.1016/j.biochi.2010.02.023 – volume: 21 start-page: 1639 year: 2014 ident: 10.1016/j.foodchem.2016.09.033_b0065 article-title: The host antimicrobial peptide Bac 7 1–35 binds to bacterial ribosomal proteins and inhibits protein synthesis publication-title: Chemistry & Biology doi: 10.1016/j.chembiol.2014.10.009 – volume: 1768 start-page: 2667 year: 2007 ident: 10.1016/j.foodchem.2016.09.033_b0030 article-title: Antimicrobial activity of histidine-rich peptides is dependent on acidic conditions publication-title: Biochimica et Biophysica Acta (BBA)-Biomembranes doi: 10.1016/j.bbamem.2007.06.020 – volume: 40 start-page: 183 year: 2011 ident: 10.1016/j.foodchem.2016.09.033_b0045 article-title: C-terminal amidation of PMAP-23: Translocation to the inner membrane of Gram-negative bacteria publication-title: Amino Acids doi: 10.1007/s00726-010-0632-1 – volume: 57 start-page: 5987 year: 2009 ident: 10.1016/j.foodchem.2016.09.033_b0130 article-title: Application of natural antimicrobials for food preservation publication-title: Journal of Agricultural and Food Chemistry doi: 10.1021/jf900668n – volume: 81 start-page: 1475 year: 2001 ident: 10.1016/j.foodchem.2016.09.033_b0180 article-title: Barrel-stave model or toroidal model? A case study on melittin pores publication-title: Biophysical Journal doi: 10.1016/S0006-3495(01)75802-X – volume: 53 start-page: 593 year: 2009 ident: 10.1016/j.foodchem.2016.09.033_b0110 article-title: Evaluation of strategies for improving proteolytic resistance of antimicrobial peptides by using variants of EFK17, an internal segment of LL-37 publication-title: Antimicrobial Agents and Chemotherapy doi: 10.1128/AAC.00477-08 – volume: 3 start-page: 608 year: 2004 ident: 10.1016/j.foodchem.2016.09.033_b0085 article-title: Trypsin cleaves exclusively C-terminal to arginine and lysine residues publication-title: Molecular & Cellular Proteomics doi: 10.1074/mcp.T400003-MCP200 – volume: 46 start-page: 867 year: 2014 ident: 10.1016/j.foodchem.2016.09.033_b0160 article-title: CecropinXJ, a silkworm antimicrobial peptide, induces cytoskeleton disruption in esophageal carcinoma cells publication-title: Acta Biochimica et Biophysica Sinica doi: 10.1093/abbs/gmu070 – volume: 10 start-page: e0131008 year: 2015 ident: 10.1016/j.foodchem.2016.09.033_b0035 article-title: Nisin ZP, a bacteriocin and food preservative, inhibits head and neck cancer tumorigenesis and prolongs survival publication-title: PLoS ONE doi: 10.1371/journal.pone.0131008 – volume: 101 start-page: 16879 year: 2004 ident: 10.1016/j.foodchem.2016.09.033_b0080 article-title: Activation of the complement system generates antibacterial peptides publication-title: Proceedings of the National Academy of Sciences of the United States of America doi: 10.1073/pnas.0406678101 – volume: 68 start-page: 2161 year: 2011 ident: 10.1016/j.foodchem.2016.09.033_b0185 article-title: Multifunctional cationic host defence peptides and their clinical applications publication-title: Cellular and Molecular Life Sciences doi: 10.1007/s00018-011-0710-x – volume: 10 start-page: 244 year: 2014 ident: 10.1016/j.foodchem.2016.09.033_b0200 article-title: Design of imperfectly amphipathic α-helical antimicrobial peptides with enhanced cell selectivity publication-title: Acta Biomaterialia doi: 10.1016/j.actbio.2013.08.043 – volume: 34 start-page: 237 year: 2013 ident: 10.1016/j.foodchem.2016.09.033_b0060 article-title: Design of hybrid β-hairpin peptides with enhanced cell specificity and potent anti-inflammatory activity publication-title: Biomaterials doi: 10.1016/j.biomaterials.2012.09.032 – volume: 18 start-page: 497 year: 2007 ident: 10.1016/j.foodchem.2016.09.033_b0090 article-title: DNA as a target for anticancer compounds: methods to determine the mode of binding and the mechanism of action publication-title: Current Opinion in Biotechnology doi: 10.1016/j.copbio.2007.09.006 – volume: 46 start-page: 2137 year: 2014 ident: 10.1016/j.foodchem.2016.09.033_b0025 article-title: Cell specificity and molecular mechanism of antibacterial and antitumor activities of carboxyl-terminal RWL-tagged antimicrobial peptides publication-title: Amino Acids doi: 10.1007/s00726-014-1761-8 – volume: 1838 start-page: 2985 year: 2014 ident: 10.1016/j.foodchem.2016.09.033_b0115 article-title: Relationship between peptide structure and antimicrobial activity as studied by de novo designed peptides publication-title: Biochimica et Biophysica Acta (BBA)-Biomembranes doi: 10.1016/j.bbamem.2014.08.018 – volume: 19 start-page: 10803 year: 2014 ident: 10.1016/j.foodchem.2016.09.033_b0125 article-title: Effects of single amino acid substitution on the biophysical properties and biological activities of an amphipathic α-helical antibacterial peptide against Gram-negative bacteria publication-title: Molecules doi: 10.3390/molecules190810803 – volume: 237 start-page: 377 year: 2004 ident: 10.1016/j.foodchem.2016.09.033_b0135 article-title: Lactoferricin B inhibits bacterial macromolecular synthesis in Escherichia coli and Bacillus subtilis publication-title: FEMS Microbiology Letters – volume: 2 start-page: 112 year: 2013 ident: 10.1016/j.foodchem.2016.09.033_b0190 article-title: Preventing breast cancer growth by cationic cecropin B publication-title: Biological System – volume: 38 start-page: 255 year: 2012 ident: 10.1016/j.foodchem.2016.09.033_b0105 article-title: Antimicrobial activity of human β-defensin 4 analogs: Insights into the role of disulfide linkages in modulating activity publication-title: Peptides doi: 10.1016/j.peptides.2012.08.024 – volume: 111 start-page: 3051 year: 1989 ident: 10.1016/j.foodchem.2016.09.033_b0095 article-title: Mixed-ligand complexes of ruthenium (II): Factors governing binding to DNA publication-title: Journal of the American Chemical Society doi: 10.1021/ja00190a046 – volume: 49 start-page: 3208 year: 2005 ident: 10.1016/j.foodchem.2016.09.033_b0020 article-title: Activity of the de novo engineered antimicrobial peptide WLBU2 against Pseudomonas aeruginosa in human serum and whole blood: Implications for systemic applications publication-title: Antimicrobial Agents and Chemotherapy doi: 10.1128/AAC.49.8.3208-3216.2005 – volume: 65 start-page: 55 year: 1983 ident: 10.1016/j.foodchem.2016.09.033_b0075 article-title: Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays publication-title: Journal of Immunological Methods doi: 10.1016/0022-1759(83)90303-4 – volume: 31 start-page: 57 year: 1993 ident: 10.1016/j.foodchem.2016.09.033_b0150 article-title: Impact of different statistical methodologies on the evaluation of the in-vitro MICs for bacteroides fragilis of selected cephalosporins and cephamycins publication-title: Journal of Antimicrobial Chemotherapy doi: 10.1093/jac/31.1.57 – volume: 90 start-page: 47 year: 2013 ident: 10.1016/j.foodchem.2016.09.033_b0155 article-title: Expression, purification and characterization of cecropin antibacterial peptide from Bombyx mori in Saccharomyces cerevisiae publication-title: Protein Expression and Purification doi: 10.1016/j.pep.2013.02.013 – volume: 1828 start-page: 443 year: 2013 ident: 10.1016/j.foodchem.2016.09.033_b0050 article-title: Antimicrobial HPA3NT3 peptide analogs: Placement of aromatic rings and positive charges are key determinants for cell selectivity and mechanism of action publication-title: Biochimica et Biophysica Acta (BBA)-Biomembranes doi: 10.1016/j.bbamem.2012.09.005 – volume: 50 start-page: 1 year: 1999 ident: 10.1016/j.foodchem.2016.09.033_b0010 article-title: Preservative agents in foods: Mode of action and microbial resistance mechanisms publication-title: International Journal of Food Microbiology doi: 10.1016/S0168-1605(99)00072-0 – volume: 9 start-page: 671 year: 2012 ident: 10.1016/j.foodchem.2016.09.033_b0100 article-title: NIH Image to ImageJ: 25 years of image analysis publication-title: Nature Methods doi: 10.1038/nmeth.2089
SSID	ssj0002018
Score	2.333145
Snippet	•CecXJ-37N shows small MICs (0.25–7.8μM) against 8 food-borne pathogenic strains.•CecXJ-37N shows low hemolysis and no cytotoxicity to normal mammalian... The antibacterial activities and mechanism of an amide-modified peptide CecXJ-37N were investigated in this study. CecXJ-37N showed small MICs (0.25-7.8μM)... The antibacterial activities and mechanism of an amide-modified peptide CecXJ-37N were investigated in this study. CecXJ-37N showed small MICs (0.25–7.8μM)...
SourceID	proquest pubmed crossref elsevier
SourceType	Aggregation Database Index Database Enrichment Source Publisher
StartPage	576
SubjectTerms	Amide modification Animals Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - pharmacology antibacterial properties Antimicrobial Cationic Peptides - chemistry Antimicrobial Cationic Peptides - pharmacology Antimicrobial peptide Cell Membrane - drug effects Cell membrane penetration Cell Survival - drug effects cytoplasm cytotoxicity DNA DNA intercalation DNA, Bacterial - chemistry Escherichia coli Escherichia coli - drug effects flow cytometry fluorescence microscopy food biopreservatives Food Contamination - prevention & control food industry Food Microbiology Food preservative Food Preservatives - chemistry Food Preservatives - pharmacology Food-borne pathogen genome Genome, Bacterial hydrolysis mechanism of action Mice Microbial Sensitivity Tests Molecular Structure NIH 3T3 Cells novel foods nucleotides pepsin scanning electron microscopy trypsin ultraviolet-visible spectroscopy
Title	A potential food biopreservative, CecXJ-37N, non-covalently intercalates into the nucleotides of bacterial genomic DNA beyond membrane attack
URI	https://dx.doi.org/10.1016/j.foodchem.2016.09.033 https://www.ncbi.nlm.nih.gov/pubmed/27664674 https://www.proquest.com/docview/1823452828 https://www.proquest.com/docview/2000201003
Volume	217
WOSCitedRecordID	wos000384851800074&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
hasFullText	1
inHoldings	1
isFullTextHit
isPrint
journalDatabaseRights	– providerCode: PRVESC databaseName: Elsevier SD Freedom Collection Journals 2021 customDbUrl: eissn: 1873-7072 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0002018 issn: 0308-8146 databaseCode: AIEXJ dateStart: 19950101 isFulltext: true titleUrlDefault: https://www.sciencedirect.com providerName: Elsevier
link	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1bb9MwFLZ2QYIXBONWLpOREC9bWBsnsf1YbUNQoYqHIeUtsl1HStUlVZtW24_gn_AjOY7tNAzK2AMvUePajp3zxecc-1wQescoMUFbTDxt3g9A_5IBl6DzsIjISOk-F9omm6DjMUtT_nVn54f3hVnPaFmyqys-_6-khjIgtnGdvQO5206hAH4D0eEKZIfrPxF-eDSvamMD1LgmViBgFk2mE7v7uraWf1qlI_jqmzP-sioDVcEQoNHsugkgsQDKGSHU3FjZtDRxj6u6mNggtdIGeYZHmCCvxr7-bDw8ktYd5lJfgg4O0quoa-GC7reZQGFAyieZa62BipUV5o1PsXC8dFM-Wm3shhrjg1FRXovKl6XW3vdLMS10dxMDGKNJqRJ31jrSZ5vdSLcwh9ar0y2tMU06XDq2ieV-YwB2L2L6wbxfMxtjvJfYSLZkw_L8Mf8NTtjaJ3rTt2nm-8lMP1mfZ9DPLtoPacxhDd0ffj5PRy3nhzrMnlrZyXQ80v88om3C0DZlpxF6Lh6hh05bwUOLssdoR5cH6P6pp98B6p0VusbvsQsvO8Njn90B6nmn9-UT9H2IW1RiM0Z8A5XHuMXkMf4VkbiLSHNTYUAk7iASVzluEYkdIjEgEltEYo9IbBH5FH37eH5x-ilwmUACFRFWB0bI1vGEcUWkkjJmmgySGITTCaPAcqVmOiI5l4TQUPepgD8F44mY0Hwg9YCSZ2gPhq5fICxgYSKhihKR8EhFE84UaCCC5jnI-rke9FDsSZIpFybfZGuZZX8HRQ-dtO3mNlDMrS24p3jmxF0rxmYA5lvbvvUQyYDi5pAPXmK1WmYDFpIoNhsp2-uEFqvA0HvoucVXO-aQJonJQPTyzvN5hR5sPu3XaK9erPQbdE-t62K5OES7NGWH7ov5CaVL8dA
linkProvider	Elsevier
openUrl	ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=A+potential+food+biopreservative%2C+CecXJ-37N%2C+non-covalently+intercalates+into+the+nucleotides+of+bacterial+genomic+DNA+beyond+membrane+attack&rft.jtitle=Food+chemistry&rft.au=Liu%2C+Dongliang&rft.au=Liu%2C+Jun&rft.au=Li%2C+Jinyao&rft.au=Xia%2C+Lijie&rft.date=2017-02-15&rft.issn=0308-8146&rft.volume=217&rft.spage=576&rft.epage=584&rft_id=info:doi/10.1016%2Fj.foodchem.2016.09.033&rft.externalDBID=n%2Fa&rft.externalDocID=10_1016_j_foodchem_2016_09_033
thumbnail_l	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0308-8146&client=summon
thumbnail_m	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0308-8146&client=summon
thumbnail_s	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0308-8146&client=summon