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Colloids Surf B Biointerfaces. 2015 Jan 1;125:213-21. doi: 10.1016/j.colsurfb.2014.11.040. Epub 2014 Dec 3.

Framework effect of amphiphilic polyesters on their molecular movement and protein adsorption-resistance properties.

Author information

1
College of Polymer Science and Engineering, Sichuan University, Chengdu 610065, China; National Engineering Research Center for Biomaterials, Sichuan University, Chengdu 610065, China.
2
College of Polymer Science and Engineering, Sichuan University, Chengdu 610065, China.
3
Institute of Biomedical and Pharmaceutical Technology, Fuzhou University, Fuzhou 350116, China.
4
National Engineering Research Center for Biomaterials, Sichuan University, Chengdu 610065, China.
5
College of Polymer Science and Engineering, Sichuan University, Chengdu 610065, China; State Key Lab of Polymer Materials Engineering, Sichuan University, Chengdu 610065, China. Electronic address: Luoxl@scu.edu.cn.

Abstract

Surface chemical characteristics of biomedical polymers, which are determined by the migration and rearrangement of polymeric chains, play an important role in the protein adsorption. In this work, the relationship between the architectures of amphiphilic polyesters and their protein adsorption resistance was investigated. Three poly (ɛ-caprolactone)s containing sulfobetaines (PCL-b-PDEAS) segments with linear, four arms and six arms star-shaped architectures were synthesized with the combination of ring-opening polymerization (ROP) and atom transfer radical polymerization (ATRP). The structures of the amphiphiles were confirmed by (1)H NMR and FTIR. Water contact angles (WCA) and X-ray photoelectron spectroscopy (XPS) were used to study the surface properties of the amphiphilic copolymer films. The water contact angles were decreased due to the surface migration of hydrophilic segments. Transmission electron microscopy (TEM) displayed the occurrence of microphase separation phenomena for PCL-b-PDEAS above glass transition temperature (Tg). The results showed that the hydrophilic segments in the copolymers would migrate to the surface of the films, which resulted in the surface more hydrophilic to resist protein adsorption. The adsorption of both fibrinogen (Fg) and bovine serum albumin (BSA) were studied. The results showed that protein adsorption was depended on not only the hydrophilic chain migration but also the shape of proteins.

KEYWORDS:

Free water fraction; Migration; Protein-adsorption; Reorganization; Sulfobetaine-based polyesters

PMID:
25499227
DOI:
10.1016/j.colsurfb.2014.11.040
[Indexed for MEDLINE]

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