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Surface‐Nucleated Assembly of Fibrillar Extracellular Matrices
Author(s) -
Capadona J. R.,
Petrie T. A.,
Fears K. P.,
Latour R. A.,
Collard D. M.,
García A. J.
Publication year - 2005
Publication title -
advanced materials
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 10.707
H-Index - 527
eISSN - 1521-4095
pISSN - 0935-9648
DOI - 10.1002/adma.200500959
Subject(s) - fibronectin , oligopeptide , covalent bond , extracellular matrix , nucleation , extracellular , materials science , sequence (biology) , domain (mathematical analysis) , biophysics , nanotechnology , crystallography , biochemistry , peptide , chemistry , biology , organic chemistry , mathematics , mathematical analysis
Synthetic surfaces , presenting a covalently immobilized oligopeptide sequence (FN13) from the self‐assembly domain of fibronectin (FN), nucleate and template the assembly of robust fibrillar extracellular matrices. These matrices contain fibronectin and type I collagen (COL), as shown in the Figure, and exhibit increased cell‐proliferation rates.