4.2 Review

Fibrillar Peptide Gels in Biotechnology and Biomedicine

Journal

BIOPOLYMERS
Volume 94, Issue 1, Pages 49-59

Publisher

WILEY
DOI: 10.1002/bip.21326

Keywords

peptides; peptidomimetics; crosslinking; biomaterials

Funding

  1. National Science Foundation [CHE-0802286]
  2. National Institutes of Health (NIDCR, NIBIB) [DE017703, EB007135]
  3. American Heart Association
  4. [0665218B]
  5. NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING [R21EB007335, R01EB009701] Funding Source: NIH RePORTER
  6. NATIONAL INSTITUTE OF DENTAL &CRANIOFACIAL RESEARCH [R21DE017703] Funding Source: NIH RePORTER
  7. Direct For Mathematical & Physical Scien [0802286] Funding Source: National Science Foundation

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Peptides, peptidomimetics, and peptide derivatives that self-assemble into fibrillar gels have received increasing interest as synthetic extracellular matrices for applications in 3D cell culture and regenerative medicine. Recently, several of these fibrillizing molecules have been functionalized with bioactive components and chemical features such as cell-binding ligands, degradable sequences, drug eluting compounds, and cross-linkable groups, thereby producing gels that can reliably display multiple factors simultaneously, This capacity for incorporating precise levels of many different biological and chemical factors is advantageous given the natural complexity of cell-matrix interactions that many current biomaterial strategies seek to mimic. In this review, recent efforts in the area of fibril-forming peptide materials are described, and advantages of biomaterials containing multiple modular elements are outlined. fit addition, a few hurdles and open questions surrounding fibrillar peptide gels are discussed, including issues of the materials' structural heterogeneity challenges in fully characterizing the diversity of their self-assembled structures, and incomplete knowledge of how the materials are processed in vivo. (C) 2010 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 94: 49-59, 2010.

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