Facile modification of collagen directed by collagen mimetic peptides.
Recent widespread interest in the development of engineered tissue and organ replacement therapies has prompted demand for new approaches to immobilize exogenous components to natural collagen. Chemical coupling of synthetic moieties to amino acid side chains has been commonly practiced for such purposes; however, such coupling reactions are difficult to control on large proteins and are generally not conducive to modifying integrated collagen scaffolds that contain live cells and tissues. As an alternative to the conventional "covalent" modification method, we have developed a novel "physical" modification technique that is based on collagen's native ability to associate into a triple-helical molecular architecture. Here, we present a finding that collagen mimetic peptides (CMPs) of sequence -(Pro-Hyp-Gly)x- exhibit strong affinity to both native and gelatinized type I collagen under controlled thermal conditions. We also show that the cell adhesion characteristics of collagen can be readily altered by applying a poly(ethylene glycol)-CMP conjugate to a prefabricated collagen film.
Wang
Allen Y
AY
Department of Materials Science and Engineering, Biomedical Engineering, and Chemistry, Johns Hopkins University, Baltimore, Maryland 21218, USA.
Mo
Xiao
X
Chen
Christopher S
CS
Yu
Seungju M
SM
D000818:Animals; D040761:Biomimetic Materials / Q000737:chemistry* / Q000378:metabolism; D001940:Breast / Q000166:cytology; D002417:Cattle; D002942:Circular Dichroism; D024042:Collagen Type I / Q000737:chemistry* / Q000378:metabolism; D004847:Epithelial Cells / Q000166:cytology; D005347:Fibroblasts / Q000166:cytology; D005453:Fluorescence; D006801:Humans; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D011092:Polyethylene Glycols / Q000737:chemistry / Q000378:metabolism; D011489:Protein Denaturation; D017433:Protein Structure, Secondary
D024042:Collagen Type I; D010455:Peptides; D011092:Polyethylene Glycols