Synthetic collagen mimics: self-assembly of homotrimers, heterotrimers and higher order structuresPart of the peptide- and protein-based materials themed issue
Collagen is a fascinating system of proteins that undergo a multi-step, hierarchical self-assembly which starts from individual peptide chains that assemble into a canonical triple helix. These triple helices then assemble into higher order structures which are often, but not always, fibrous in natu...
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| Main Authors | , , |
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| Format | Journal Article |
| Language | English |
| Published |
18.08.2010
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| Online Access | Get full text |
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| Summary: | Collagen is a fascinating system of proteins that undergo a multi-step, hierarchical self-assembly which starts from individual peptide chains that assemble into a canonical triple helix. These triple helices then assemble into higher order structures which are often, but not always, fibrous in nature. While collagen is the most abundant protein in the human body, the details of its structure and mechanism of assembly are surprisingly poorly understood. This
critical review
will focus on small peptide systems, commonly referred to as collagen mimetic peptides (CMPs) which have been used successfully to help unravel some of the mystery of this complex structure. We will discuss homotrimeric CMPs, which are the most commonly researched subject in this field, and the structure of the collagen triple helix in detail and the factors that contribute to its stabilization. We will also cover how CMPs have been used to study breaks in triple helical domains as models for connective tissue diseases and, finally, how they have been used to understand the interactions of collagenous proteins with cell-surface receptors. Additionally, we will focus on heterotrimeric CMPs, a relatively new area of collagen research. Finally, we will deal with CMPs used as models for higher level self-assembly and also as materials that are designed to mimic the function of collagens in the extracellular matrix (178 references).
This critical review focuses on small peptide systems, commonly referred to as collagen mimetic peptides, which have been used successfully to understand the structure, biochemistry, and self-assembly of natural collagen. |
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| Bibliography: | Part of the peptide- and protein-based materials themed issue. Prof. Jeffrey D. Hartgerink received his PhD in 1999 from the Scripps Research Institute under the guidance of M. Reza Ghadiri and completed a postdoctoral fellowship from Northwestern University in 2002 with Samuel I. Stupp. After this, he joined the faculty at Rice University as an assistant professor in the departments of Chemistry and Bioengineering and in 2008 was promoted to associate professor. Jeff's research focuses on the self-assembly of peptide based materials organized in micelles, alpha-helices, beta-sheets, collagen-like motifs. In his lab these materials are used both to gain insight into the supramolecular interactions driving their folding and assembly as well as their biomedical application. Lesley O'Leary received her BS degree in Chemistry from the University of Richmond in 2006. She received her masters in Chemistry from Rice University in 2009 and is currently pursuing her PhD degree in Chemistry from Rice University under the supervision of Professor Jeffrey Hartgerink. Her research interests are in the fields of supramolecular chemistry and more specifically at the design and hierarchical self-assembly of collagen mimetic peptides. Jorge Fallas received his BS degree in Chemistry from the Freie Universitaet zu Berlin in 2007. He received his masters in Chemistry from Rice University in 2009 and is currently pursuing his PhD degree at the same university under the supervision of Prof. Jeffrey Hartgerink. His current research interests are in the design and structural determination of supramolecular assemblies specifically collagen mimetic peptides. |
| ISSN: | 0306-0012 1460-4744 |
| DOI: | 10.1039/b919455j |