TY - JOUR
T1 - Evaluation of in situ albumin binding surfaces
T2 - A study of protein adsorption and platelet adhesion
AU - Guha Thakurta, Sanjukta
AU - Subramanian, Anuradha
N1 - Funding Information:
Acknowledgments This work was partially supported by NSF Grant CTS-0411632 and Army Research Laboratory W911NF-04-2-0011. We are thankful to Gaye Homer, University of Nebraska Health Center, Lincoln, NE for letting us use the platelet counting instrument; Dr. H. Chen and Dr. Y. Joe. Zhou of microscopy facility of Center of Biotechnology; Dr. D. W. Thompson and Dr. T. Hofmann of Center for Materials Research and Analysis, University of
PY - 2011/1
Y1 - 2011/1
N2 - Surface modification strategies that take advantage of the passivation effects of albumin are important in the development of biomaterial surfaces. In this study, linear peptides (LP1, LP2) and a small chemical ligand (SCL) with albumin binding affinities were grafted onto silane functionalized silicon substrates. Surfaces were characterized with contact angle and ellipsometric measurements, and densities of immobilized ligands were assessed spectroscopically. Ellipsometrically measured thickness correlated with the predicted molecular lengths of grafted moieties. Contact angle analysis indicated that the LP1 and LP2 functionalized surfaces were hydrophilic compared to SCL functionalized and control surfaces. Adsorption of albumin from human serum was evaluated and quantified via specific enzyme-linked immunosorbent assays and 2D gel electrophoresis. The following trend was noted for surface adsorbed albumin: LP1 > LP2 > SCL > C, with LP1 derivatized surfaces having ~2.450 μg/cm2 of bound albumin. LP1 derivatized surfaces possessed the least number of adsorbed platelets with rounded platelet morphology when compared to control surface.
AB - Surface modification strategies that take advantage of the passivation effects of albumin are important in the development of biomaterial surfaces. In this study, linear peptides (LP1, LP2) and a small chemical ligand (SCL) with albumin binding affinities were grafted onto silane functionalized silicon substrates. Surfaces were characterized with contact angle and ellipsometric measurements, and densities of immobilized ligands were assessed spectroscopically. Ellipsometrically measured thickness correlated with the predicted molecular lengths of grafted moieties. Contact angle analysis indicated that the LP1 and LP2 functionalized surfaces were hydrophilic compared to SCL functionalized and control surfaces. Adsorption of albumin from human serum was evaluated and quantified via specific enzyme-linked immunosorbent assays and 2D gel electrophoresis. The following trend was noted for surface adsorbed albumin: LP1 > LP2 > SCL > C, with LP1 derivatized surfaces having ~2.450 μg/cm2 of bound albumin. LP1 derivatized surfaces possessed the least number of adsorbed platelets with rounded platelet morphology when compared to control surface.
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U2 - 10.1007/s10856-010-4169-3
DO - 10.1007/s10856-010-4169-3
M3 - Article
C2 - 21120589
AN - SCOPUS:78751566802
SN - 0957-4530
VL - 22
SP - 137
EP - 149
JO - Journal of Materials Science: Materials in Medicine
JF - Journal of Materials Science: Materials in Medicine
IS - 1
ER -