Adsorption of albumin and sodium hyaluronate on UHMWPE: A QCM-D and AFM study

被引:37
|
作者
Serro, A. P. [1 ,2 ]
Degiampietro, K. [1 ]
Colaco, R. [3 ]
Saramago, B. [1 ]
机构
[1] Univ Tecn Lisboa, Ctr Quim Estrutural, Inst Super Tecn, P-1049001 Lisbon, Portugal
[2] Inst Super Ciencias Saude Egas Moniz, Ctr Invest Interdisciplinar Egas Moniz, P-2829511 Caparica, Portugal
[3] Univ Tecn Lisboa, Dept Mat Engn, Inst Super Tecn, P-1049001 Lisbon, Portugal
关键词
UHMWPE; Albumin; Hyaluronic acid; Adsorption; Adhesion force; Wettability; MOLECULAR-WEIGHT POLYETHYLENE; ATOMIC-FORCE MICROSCOPY; HUMAN SERUM-ALBUMIN; L-HISTIDINE LIGAND; PROTEIN ADSORPTION; BOUNDARY LUBRICATION; SURFACE WETTABILITY; JOINT MATERIALS; SYNOVIAL-FLUID; HIP-PROSTHESIS;
D O I
10.1016/j.colsurfb.2010.01.022
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
The biotribological properties of artificial joints, in particular the efficiency of the lubrication, strongly determine their lifetime. The most commonly used artificial joints combine a metallic or ceramic part articulating against a ultra high molecular weight polyethylene (UHMWPE) counterface. and are lubricated by the periprosthetic fluid. This fluid contains several macromolecules, namely albumin and sodium hyaluronate (NaHA), that are known to be involved in the lubrication process. There are several studies in the literature concerning the interaction of the referred macromolecules with ceramic or metallic prosthetic materials. However, to our knowledge, information about their binding to the polymeric surface is practically inexistent. The objective of this work is to contribute to clarify the role played by albumin and NaHA on the biolubrication process, through the investigation of their interaction with the UHMWPE surface. The study involves adsorption measurements using a quartz crystal microbalance with dissipation (QCM-D), the characterization of the adsorbed films by atomic force microscopy (AFM) and wettability determinations. Albumin was found to adsorb strongly and extensively to the polymer, while NaHA led to a very low adsorption. In both cases rigid films were obtained, but with different morphology and porosity. The high binding affinity of the protein to the polymer was demonstrated both by the results of the fittings to Langmuir and Freundlich models and by the values of the adhesion forces determined by AFM. In the simultaneous adsorption of albumin and NaHA, protein adsorption is predominant and determines the surface properties. (C) 2010 Elsevier B.V. All rights reserved.
引用
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页码:1 / 7
页数:7
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