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

Abstract:

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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:

Zhong Wei Gu, Yafang Han, Fu Sheng Pan, Xitao Wang, Duan Weng and Shaoxiong Zhou

Pages:

1219-1223

DOI:

10.4028/www.scientific.net/MSF.610-613.1219

Citation:

R. Zeng et al., "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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$35.00

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