Literature DB >> 16147856

Triple helical collagen-like peptides: engineering and applications in matrix biology.

Takaki Koide1.   

Abstract

Collagen, a large insoluble protein with a characteristic triple helical structure, is found as the most prominent component of extracellular matrix. The functions of collagen are not limited to providing mechanical strength to various tissues and organs as a structural protein, as it has been pointed out that collagen exhibits various biological functions through specific interactions with other macromolecules. However, the use of native triple helical collagen is often troublesome because of its insolubility and gelating properties. Instead, triple helical collagen-like peptides have been designed and are used as collagen surrogates in studies on collagen structure, stability, and biological functions including binding to other proteins and cultured cells. This article reviews recent progress in peptide design, synthesis, and the applications of collagen-like peptides in current matrix biology, while emphasizing the advantages of the peptide-based strategy.

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Year:  2005        PMID: 16147856     DOI: 10.1080/03008200591008518

Source DB:  PubMed          Journal:  Connect Tissue Res        ISSN: 0300-8207            Impact factor:   3.417


  11 in total

Review 1.  Biological matrices and bionanotechnology.

Authors:  Patricia M Taylor
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2007-08-29       Impact factor: 6.237

2.  Stabilization of collagen-model, triple-helical peptides for in vitro and in vivo applications.

Authors:  Manishabrata Bhowmick; Gregg B Fields
Journal:  Methods Mol Biol       Date:  2013

Review 3.  Synthesis and biological applications of collagen-model triple-helical peptides.

Authors:  Gregg B Fields
Journal:  Org Biomol Chem       Date:  2010-01-20       Impact factor: 3.876

4.  Evaluation of Therapeutic Collagen-Based Biomaterials in the Infarcted Mouse Heart by Extracellular Matrix Targeted MALDI Imaging Mass Spectrometry.

Authors:  Cassandra L Clift; Sarah McLaughlin; Marcelo Muñoz; Erik J Suuronen; Benjamin H Rotstein; Anand S Mehta; Richard R Drake; Emilio I Alarcon; Peggi M Angel
Journal:  J Am Soc Mass Spectrom       Date:  2021-10-29       Impact factor: 3.109

Review 5.  Production of self-assembling biomaterials for tissue engineering.

Authors:  Stuart Kyle; Amalia Aggeli; Eileen Ingham; Michael J McPherson
Journal:  Trends Biotechnol       Date:  2009-06-06       Impact factor: 19.536

6.  Spatio-temporal modification of collagen scaffolds mediated by triple helical propensity.

Authors:  Allen Y Wang; Catherine A Foss; Shirley Leong; Xiao Mo; Martin G Pomper; Seungju M Yu
Journal:  Biomacromolecules       Date:  2008-06-12       Impact factor: 6.988

7.  The Yersinia adhesin YadA binds to a collagenous triple-helical conformation but without sequence specificity.

Authors:  Jack C Leo; Heli Elovaara; Barbara Brodsky; Mikael Skurnik; Adrian Goldman
Journal:  Protein Eng Des Sel       Date:  2008-05-07       Impact factor: 1.650

8.  The synthesis and coupling of photoreactive collagen-based peptides to restore integrin reactivity to an inert substrate, chemically-crosslinked collagen.

Authors:  Jean-Daniel Malcor; Daniel Bax; Samir W Hamaia; Natalia Davidenko; Serena M Best; Ruth E Cameron; Richard W Farndale; Dominique Bihan
Journal:  Biomaterials       Date:  2016-01-23       Impact factor: 12.479

9.  Supramolecular Nanofibers from Collagen-Mimetic Peptides Bearing Various Aromatic Groups at N-Termini via Hierarchical Self-Assembly.

Authors:  Tomoyuki Koga; Shinya Kingetsu; Nobuyuki Higashi
Journal:  Int J Mol Sci       Date:  2021-04-26       Impact factor: 5.923

Review 10.  Peptide-Based Functional Biomaterials for Soft-Tissue Repair.

Authors:  Katsuhiro Hosoyama; Caitlin Lazurko; Marcelo Muñoz; Christopher D McTiernan; Emilio I Alarcon
Journal:  Front Bioeng Biotechnol       Date:  2019-08-23
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