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- W2921135500 endingPage "252" @default.
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- W2921135500 abstract "The triple-helical structure of collagen has been accurately reproduced in numerous chemical and recombinant model systems. Triple-helical peptides have found application for dissecting collagen-stabilizing forces, isolating receptor and protein binding sites in collagen, evaluating collagen-mediated cell signaling activities, mechanistic examination of collagenolytic proteases, and developing novel biomaterials and drug delivery vehicles. Due to their inherent stability to general proteolysis, triple-helical peptides present an opportunity as in vivo inhibitory agents. The present chapter provides methods for the construction of collagen-based triple-helical peptides designed as matrix metalloproteinase inhibitors." @default.
- W2921135500 created "2019-03-22" @default.
- W2921135500 creator A5068707393 @default.
- W2921135500 date "2019-01-01" @default.
- W2921135500 modified "2023-09-27" @default.
- W2921135500 title "Methods for the Construction of Collagen-Based Triple-Helical Peptides Designed as Matrix Metalloproteinase Inhibitors" @default.
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- W2921135500 doi "https://doi.org/10.1007/978-1-4939-9095-5_17" @default.
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