MMP-9 triggered self-assembly of doxorubicin nanofiber depots halts tumor growth

A central challenge in cancer care is to ensure that therapeutic compounds reach their targets. One approach is to use enzyme-responsive biomaterials, which reconfigure in response to endogenous enzymes that are overexpressed in diseased tissues, as potential site-specific anti-tumoral therapies. He...

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Veröffentlicht in:	Biomaterials Jg. 98; S. 192 - 202
Hauptverfasser:	Kalafatovic, Daniela, Nobis, Max, Son, Jiye, Anderson, Kurt I., Ulijn, Rein V.
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	Netherlands Elsevier Ltd 01.08.2016
Schlagworte:	Advanced Basic Science animal models Animals biocompatible materials Biomaterials Biomedical materials Cancer therapy Cell Line, Tumor Cell Proliferation - drug effects Dentistry Doxorubicin Doxorubicin - pharmacology Doxorubicin - therapeutic use Drug Carriers - chemistry Enzymes Humans hydrolysis Matrix Metalloproteinase 9 - metabolism Mice, Nude Micelles MMP Morphology transition nanofibers Nanofibers - chemistry Nanofibers - ultrastructure Nanostructure Neoplasm Invasiveness neoplasms Neoplasms - drug therapy Neoplasms - pathology Peptides Peptides - pharmacology Self assembly Surgical implants tissues Tumors MMP Self-assembly Peptides Morphology transition Cancer therapy
ISSN:	0142-9612, 1878-5905, 1878-5905
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Abstract	A central challenge in cancer care is to ensure that therapeutic compounds reach their targets. One approach is to use enzyme-responsive biomaterials, which reconfigure in response to endogenous enzymes that are overexpressed in diseased tissues, as potential site-specific anti-tumoral therapies. Here we report peptide micelles that upon MMP-9 catalyzed hydrolysis reconfigure to form fibrillar nanostructures. These structures slowly release a doxorubicin payload at the site of action. Using both in vitro and in vivo models, we demonstrate that the fibrillar depots are formed at the sites of MMP-9 overexpression giving rise to enhanced efficacy of doxorubicin, resulting in inhibition of tumor growth in an animal model.
AbstractList	A central challenge in cancer care is to ensure that therapeutic compounds reach their targets. One approach is to use enzyme-responsive biomaterials, which reconfigure in response to endogenous enzymes that are overexpressed in diseased tissues, as potential site-specific anti-tumoral therapies. Here we report peptide micelles that upon MMP-9 catalyzed hydrolysis reconfigure to form fibrillar nanostructures. These structures slowly release a doxorubicin payload at the site of action. Using both in vitro and in vivo models, we demonstrate that the fibrillar depots are formed at the sites of MMP-9 overexpression giving rise to enhanced efficacy of doxorubicin, resulting in inhibition of tumor growth in an animal model. A central challenge in cancer care is to ensure that therapeutic compounds reach their targets. One approach is to use enzyme-responsive biomaterials, which reconfigure in response to endogenous enzymes that are overexpressed in diseased tissues, as potential site-specific anti-tumoral therapies. Here we report peptide micelles that upon MMP-9 catalyzed hydrolysis reconfigure to form fibrillar nanostructures. These structures slowly release a doxorubicin payload at the site of action. Using both in vitro and in vivo models, we demonstrate that the fibrillar depots are formed at the sites of MMP-9 overexpression giving rise to enhanced efficacy of doxorubicin, resulting in inhibition of tumor growth in an animal model. A central challenge in cancer care is to ensure that therapeutic compounds reach their targets. One approach is to use enzyme-responsive biomaterials, which reconfigure in response to endogenous enzymes that are overexpressed in diseased tissues, as potential site-specific anti-tumoral therapies. Here we report peptide micelles that upon MMP-9 catalyzed hydrolysis reconfigure to form fibrillar nanostructures. These structures slowly release a doxorubicin payload at the site of action. Using both in vitro and in vivo models, we demonstrate that the fibrillar depots are formed at the sites of MMP-9 overexpression giving rise to enhanced efficacy of doxorubicin, resulting in inhibition of tumor growth in an animal model.A central challenge in cancer care is to ensure that therapeutic compounds reach their targets. One approach is to use enzyme-responsive biomaterials, which reconfigure in response to endogenous enzymes that are overexpressed in diseased tissues, as potential site-specific anti-tumoral therapies. Here we report peptide micelles that upon MMP-9 catalyzed hydrolysis reconfigure to form fibrillar nanostructures. These structures slowly release a doxorubicin payload at the site of action. Using both in vitro and in vivo models, we demonstrate that the fibrillar depots are formed at the sites of MMP-9 overexpression giving rise to enhanced efficacy of doxorubicin, resulting in inhibition of tumor growth in an animal model. Abstract A central challenge in cancer care is to ensure that therapeutic compounds reach their targets. One approach is to use enzyme-responsive biomaterials, which reconfigure in response to endogenous enzymes that are overexpressed in diseased tissues, as potential site-specific anti-tumoral therapies. Here we report peptide micelles that upon MMP-9 catalyzed hydrolysis reconfigure to form fibrillar nanostructures. These structures slowly release a doxorubicin payload at the site of action. Using both in vitro and in vivo models, we demonstrate that the fibrillar depots are formed at the sites of MMP-9 overexpression giving rise to enhanced efficacy of doxorubicin, resulting in inhibition of tumor growth in an animal model.
Author	Kalafatovic, Daniela Nobis, Max Son, Jiye Ulijn, Rein V. Anderson, Kurt I.
Author_xml	– sequence: 1 givenname: Daniela surname: Kalafatovic fullname: Kalafatovic, Daniela email: daniela.kalafatovic@irbbarcelona.org organization: Advanced Science Research Center (ASRC), City University New York, 85 St Nicholas Terrace, New York, NY 10031, USA – sequence: 2 givenname: Max surname: Nobis fullname: Nobis, Max organization: CRUK Beatson Institute, Garscube Estate, Glasgow, G61 1BD, UK – sequence: 3 givenname: Jiye surname: Son fullname: Son, Jiye organization: Advanced Science Research Center (ASRC), City University New York, 85 St Nicholas Terrace, New York, NY 10031, USA – sequence: 4 givenname: Kurt I. surname: Anderson fullname: Anderson, Kurt I. email: kurt.anderson@crick.ac.uk organization: CRUK Beatson Institute, Garscube Estate, Glasgow, G61 1BD, UK – sequence: 5 givenname: Rein V. surname: Ulijn fullname: Ulijn, Rein V. email: Rein.Ulijn@asrc.cuny.edu organization: Advanced Science Research Center (ASRC), City University New York, 85 St Nicholas Terrace, New York, NY 10031, USA
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Keywords	MMP Self-assembly Peptides Morphology transition Cancer therapy
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Snippet	A central challenge in cancer care is to ensure that therapeutic compounds reach their targets. One approach is to use enzyme-responsive biomaterials, which... Abstract A central challenge in cancer care is to ensure that therapeutic compounds reach their targets. One approach is to use enzyme-responsive biomaterials,...
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SubjectTerms	Advanced Basic Science animal models Animals biocompatible materials Biomaterials Biomedical materials Cancer therapy Cell Line, Tumor Cell Proliferation - drug effects Dentistry Doxorubicin Doxorubicin - pharmacology Doxorubicin - therapeutic use Drug Carriers - chemistry Enzymes Humans hydrolysis Matrix Metalloproteinase 9 - metabolism Mice, Nude Micelles MMP Morphology transition nanofibers Nanofibers - chemistry Nanofibers - ultrastructure Nanostructure Neoplasm Invasiveness neoplasms Neoplasms - drug therapy Neoplasms - pathology Peptides Peptides - pharmacology Self assembly Surgical implants tissues Tumors
Title	MMP-9 triggered self-assembly of doxorubicin nanofiber depots halts tumor growth
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