REVIEW ARTICLE
Surface Modification of SUS 316L Stainless Steel with Tartaric Acid Derivative-Crosslinked Human Serum Albumin Matrices
Sachiro Kakinoki1, Yasuyuki Katada2, Yoshiyuki Uchida1, Tetsushi Taguchi1, *
Article Information
Identifiers and Pagination:
Year: 2008Volume: 2
First Page: 143
Last Page: 147
Publisher ID: TOBIOTJ-2-143
DOI: 10.2174/1874070700802010143
Article History:
Received Date: 17/12/2007Acceptance Date: 17/12/2007
Electronic publication date: 27/5/2008
Collection year: 2008
open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: (https://creativecommons.org/licenses/by/4.0/legalcode). This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Abstract
The surface of stainless steel (SUS316L) was modified by alternating immersion in a solution of human serum albumin (HSA) and solution of a tartaric acid derivative (TAD). The resulting HSA/TAD-immobilized SUS316L was characterized by means of contact-angle measurement, attenuated total-reflectance Fourier-transform infrared spectroscopy, atomic force microscopy, and X-ray photoelectron spectroscopy. A HSA/TAD layer was formed on the surface of SUS316L, the thickness of which increased with increasing numbers of cycles of alternating immersion in the two solutions. The HSA/TAD layer on SUS316L was stable to washing in 1 M NaCl or 5 vol% sodium dodecyl sulfate, showing that the layer was immobilized by covalent bonding rather than electrostatic or hydrophobic interaction. The presence of the HSA/TAD layer on the SUS316L suppressed the formation of a fibrin network. Alternating immersion in solutions of HSA and TAD is a useful technique for functionalizing the surfaces of metals.