Literature DB >> 23131209

Development and utilization of a bovine type I collagen microfibril model.

Eleanor M Brown1.   

Abstract

The structure of fibrous collagen, a long triple helix that self-associates in a staggered array to form a matrix of fibrils, fibers and fiber bundles, makes it uniquely suitable as a scaffold for biomaterial engineering. A major challenge for this application is to stabilize collagen structure by means that are acceptable for the end use. The bovine type I collagen microfibril model, built by computer assisted modeling, comprised of five right-handed triple helices in a left-handed super coil containing gap and overlap regions as well as the nonhelical telopeptides is a tool for predicting or visualizing chemistry to stabilize the matrix, insert an active agent, or otherwise modify collagen. Published by Elsevier B.V.

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Year:  2012        PMID: 23131209     DOI: 10.1016/j.ijbiomac.2012.10.029

Source DB:  PubMed          Journal:  Int J Biol Macromol        ISSN: 0141-8130            Impact factor:   6.953


  1 in total

1.  Variation in the helical structure of native collagen.

Authors:  Joseph P R O Orgel; Anton V Persikov; Olga Antipova
Journal:  PLoS One       Date:  2014-02-24       Impact factor: 3.240

  1 in total

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