A review emphasizing on utility of heptad repeat sequence as a tool to design pharmacologically safe peptide-based antibiotics

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Názov: A review emphasizing on utility of heptad repeat sequence as a tool to design pharmacologically safe peptide-based antibiotics
Autori: Vikas, Yadav, Misra, Richa
Prispievatelia: Central Drug Research Institute, Kungliga Fysiografiska Sällskapet i Lund
Zdroj: Biochimie. 191:126-139
Informácie o vydavateľovi: Elsevier BV, 2021.
Rok vydania: 2021
Predmety: Repetitive Sequences, Amino Acid, 0301 basic medicine, Cytotoxicity, Anti-Bacterial Agents/chemistry, Antimicrobial Cationic Peptides/chemistry, Biochimie, biophysique & biologie moléculaire, Biochemistry, Sciences de la santé humaine, 03 medical and health sciences, Antimicrobial Cationic Peptides/therapeutic use, Humans, Human health sciences, Haematotoxicity, Pharmacy, pharmacology & toxicology, 0303 health sciences, Heptad repeat sequence, General Medicine, Pharmacie, pharmacologie & toxicologie, Life sciences, Anti-Bacterial Agents, 3. Good health, Anti-Bacterial Agents/therapeutic use, Leucine zipper motif, Drug Design, Sciences du vivant, Antimicrobial peptides, Phenylalanine zipper motif, Biochemistry, biophysics & molecular biology, Antimicrobial Cationic Peptides
Popis: Extensive usage of antibiotics has created an unprecedented scenario of the rapid emergence of many drug-resistant bacteria, which has become an alarming public health concern around the globe. Search for better alternatives that are as efficacious as antibiotics led to the discovery of antimicrobial peptides (AMPs). These small cationic amphiphilic peptides have emerged as a promising option as antimicrobial agents, owing to their multifaceted implications against varied pathogens. Recent years have witnessed tremendous growth in research on AMPs resulting in them being tested in clinical trials of which six got approved for topical application. The relatively less successful outcome has been attributed to the poor cell selectivity shown by most of the naturally occurring AMPs. This drawback needs to be circumvented by identifying strategies to design safe and effective peptides. In the present review, we have emphasized the importance of heptad repeat sequence (leucine and/or phenylalanine zipper motif) as a tool that has shown great promise in remodeling the toxic AMPs to safe antimicrobial agents.
Druh dokumentu: Article
Jazyk: English
ISSN: 0300-9084
DOI: 10.1016/j.biochi.2021.09.001
Prístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/34492334
https://pubmed.ncbi.nlm.nih.gov/34492334/
https://portal.research.lu.se/en/publications/a-review-emphasizing-on-utility-of-heptad-repeat-sequence-as-a-to
https://www.sciencedirect.com/science/article/pii/S0300908421002042
https://lup.lub.lu.se/search/publication/1876ff6d-36ab-4363-aae7-a9835ccd628e
Rights: CC BY
Prístupové číslo: edsair.doi.dedup.....4706f4575c71c075ce0aea53255a177d
Databáza: OpenAIRE
Popis
Abstrakt:Extensive usage of antibiotics has created an unprecedented scenario of the rapid emergence of many drug-resistant bacteria, which has become an alarming public health concern around the globe. Search for better alternatives that are as efficacious as antibiotics led to the discovery of antimicrobial peptides (AMPs). These small cationic amphiphilic peptides have emerged as a promising option as antimicrobial agents, owing to their multifaceted implications against varied pathogens. Recent years have witnessed tremendous growth in research on AMPs resulting in them being tested in clinical trials of which six got approved for topical application. The relatively less successful outcome has been attributed to the poor cell selectivity shown by most of the naturally occurring AMPs. This drawback needs to be circumvented by identifying strategies to design safe and effective peptides. In the present review, we have emphasized the importance of heptad repeat sequence (leucine and/or phenylalanine zipper motif) as a tool that has shown great promise in remodeling the toxic AMPs to safe antimicrobial agents.
ISSN:03009084
DOI:10.1016/j.biochi.2021.09.001