Paper Title:
Protein Adsorption Behaviors on PLLA Surface Studied by Quartz Crystal Microbalance with Dissipation Monitoring (QCM-D)
  Abstract

The adsorption of two different proteins (bovine serum albumin (BSA) and collagen-I) onto poly (L-lactic acid) (PLLA) surface was investigated using quartz crystal microbalance with dissipation monitoring (QCM-D) and atomic force microscopy (AFM). It’s found that protein characteristics would greatly affect the adsorption kinetics, structure and viscoelastic properties of adsorbed protein layers. Compared with BSA, collagen-I trended to form a loose, dissipative layer with a slower adsorption rate and larger adsorption reversibility, which is consistent with AFM observation. The results provided some valuable information for controlling the structure and properties of adsorbed proteins to develop an alternative surface-modification approach for biomaterials.

  Info
Periodical
Materials Science Forum (Volumes 610-613)
Main Theme
Edited by
Zhongwei Gu, Yafang Han, Fusheng Pan, Xitao Wang, Duan Weng and Shaoxiong Zhou
Pages
1219-1223
DOI
10.4028/www.scientific.net/MSF.610-613.1219
Citation
R. Zeng, Y. Zhang, M. Tu, C. R. Zhou, "Protein Adsorption Behaviors on PLLA Surface Studied by Quartz Crystal Microbalance with Dissipation Monitoring (QCM-D)", Materials Science Forum, Vols. 610-613, pp. 1219-1223, 2009
Online since
January 2009
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$32.00
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