Premium
Two‐dimensional artificial extracellular matrix: Bioadhesive peptide‐immobilized surface design
Author(s) -
Kondoh Akihiro,
Makino Keisuke,
Matsuda Takehisa
Publication year - 1993
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.1993.070471108
Subject(s) - tetrapeptide , bioadhesive , fibronectin , vinyl alcohol , adhesion , peptide , adhesive , matrix (chemical analysis) , cell adhesion , extracellular matrix , chemistry , surface modification , materials science , biophysics , polymer chemistry , polymer , chromatography , nanotechnology , biochemistry , layer (electronics) , organic chemistry , biology
A novel artificial extracellular matrix derivatized with a cell adhesive peptide, Arg—Gly—Asp—Ser (RGDS) tetrapeptide, which is the central peptidyl sequence of the adhesive site of fibronectin, was designed. RGDS coupling was achieved via isocyanation of surface hydroxyl groups of poly(vinyl alcohol) (PVA) film and subsequent conversion to activated ester. The surface‐modified PVA film was quantitatively analyzed by ESCA. The surface density of RGDS was partly controlled by the degree of isocyanation of the PVA film. Bovine endothelial cells (ECs) adhered and grew well on the RGDS‐derivatized PVA film, irrespective of the presence or absence of the serum. The adhesion and growth of ECs were enhanced with an increase in the surface density of RGDS. When a sufficient amount of RGDS was added to the medium, the adhered ECs were delaminated. This indicated that the adhesion of ECs on an RGDS‐derivatized PVA surface is mediated by the RGD—ligand/receptor interaction. Thus, a peptidyl artificial matrix via surface derivatization was developed. © 1993 John Wiley & Sons, Inc.