Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 103, Issue 9, Pages 3028-3033Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0508783103
Keywords
biomaterial; coiled-coil; nanotechnology; cystine knot; peptide
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Funding
- NCRR NIH HHS [1RR13790] Funding Source: Medline
- NIAMS NIH HHS [R01 AR044276, AR44276, F32 AR050881, AR50881] Funding Source: Medline
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Collagen is the most abundant protein in animals and the major component of connective tissues. Although collagen isolated from natural sources has long served as the basis for some biomaterials, natural collagen is difficult to modify and can engender pathogenic and immunological side effects. Collagen comprises a helix of three strands. Triple helices derived from synthetic peptides are much shorter (< 10 nm) than natural collagen (approximate to 300 mm), limiting their utility. Here, we describe the synthesis of short collagen fragments in which the three strands are held in a staggered array by disulficle bonds. Data from CD spectroscopy, dynamic light scattering, analytical ultracentrifugation, atomic force microscopy, and transmission electron microscopy indicate that these sticky-ended fragments self-assemble via intermolecular triple-helix formation. The resulting fibrils resemble natural collagen, and some are longer (> 400 nm) than any known collagen. We anticipate that our self-assembly strategy can provide synthetic collagen-mimetic materials for a variety of applications.
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