Surface Modification of SUS 316L Stainless Steel with Tartaric Acid Derivative-Crosslinked Human Serum Albumin Matrices
REVIEW ARTICLE

Surface Modification of SUS 316L Stainless Steel with Tartaric Acid Derivative-Crosslinked Human Serum Albumin Matrices

The Open Biotechnology Journal 27 May 2008 REVIEW ARTICLE DOI: 10.2174/1874070700802010143

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.