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Three‐dimensional chemical structures by protein functionalized micron‐sized beads bound to polylysine‐coated silicone surfaces
Author(s) -
Lateef Syed S.,
Boateng Samuel,
Ahluwalia Neil,
Hartman Thomas J.,
Russell Brenda,
Hanley Luke
Publication year - 2005
Publication title -
journal of biomedical materials research part a
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.849
H-Index - 150
eISSN - 1552-4965
pISSN - 1549-3296
DOI - 10.1002/jbm.a.30229
Subject(s) - polylysine , materials science , silicone , surface modification , biophysics , covalent bond , bovine serum albumin , polymer chemistry , adhesion , chemical modification , fibroblast , extracellular matrix , in vitro , chemical engineering , chromatography , chemistry , biochemistry , composite material , organic chemistry , engineering , biology
A novel method is described here that allows three‐dimensional (3D) control of both chemistry and morphology by a series of wet chemical steps: the attachment of protein functionalized micron‐sized beads onto a flat silicone surface that has been functionalized with a distinct chemical modification. Bovine serum albumin (BSA), laminin, or polylysine is covalently bound to 6.5‐μm‐diameter spherical beads. A chemical method is then used to bind these beads to a flat silicone surface that is subsequently functionalized with polylysine. This process leads to a nonspecific cell adhesive background on the flat surface (polylysine) with the option of differing chemistry on the third‐dimension due to the protein BSA or laminin on the bead protruding from the surface. The beads do not detach during cyclic stretching in vitro . Neo‐natal rat cardiac fibroblasts are cultured on the beaded surfaces and compared with fibroblasts cultured on nonbeaded, flat polylysine surfaces. Fibroblast plating density, integrin, and physical responses are examined as a function of varying the ligands on the beads. © 2005 Wiley Periodicals, Inc. J Biomed Mater Res 72A: 373–380, 2005