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Free radical functionalization of surfaces to prevent adverse responses to biomedical devices.

Abstract：

:Immobilizing a protein, that is fully compatible with the patient, on the surface of a biomedical device should make it possible to avoid adverse responses such as inflammation, rejection, or excessive fibrosis. A surface that strongly binds and does not denature the compatible protein is required. Hydrophilic surfaces do not induce denaturation of immobilized protein but exhibit a low binding affinity for protein. Here, we describe an energetic ion-assisted plasma process that can make any surface hydrophilic and at the same time enable it to covalently immobilize functional biological molecules. We show that the modification creates free radicals that migrate to the surface from a reservoir beneath. When they reach the surface, the radicals form covalent bonds with biomolecules. The kinetics and number densities of protein molecules in solution and free radicals in the reservoir control the time required to form a full protein monolayer that is covalently bound. The shelf life of the covalent binding capability is governed by the initial density of free radicals and the depth of the reservoir. We show that the high reactivity of the radicals renders the binding universal across all biological macromolecules. Because the free radical reservoir can be created on any solid material, this approach can be used in medical applications ranging from cardiovascular stents to heart-lung machines.

journal_name

Proc Natl Acad Sci U S A

journal_title

Proceedings of the National Academy of Sciences of the United States of America

authors

Bilek MM,Bax DV,Kondyurin A,Yin Y,Nosworthy NJ,Fisher K,Waterhouse A,Weiss AS,dos Remedios CG,McKenzie DR

doi

10.1073/pnas.1103277108

subject

Has Abstract

pub_date

2011-08-30 00:00:00

pages

14405-10

issue

35

eissn

0027-8424

issn

1091-6490

pii

1103277108

journal_volume

108

pub_type

杂志文章

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