Bovine Serum Albumin and Fibrinogen Adsorption at the 316L Stainless Steel/Aqueous Interface

The binding of bovine serum albumin (BSA) to a 316L stainless steel surface from a buffer solution has been characterized using neutron reflectometry and quartz crystal microbalance measurements; coverage at all concentrations up to a near-physiological concentration was found to be relatively low (

Saved in:
Bibliographic Details
Published in:The journal of physical chemistry. B 2018-05, Vol.122 (19), p.5057-5065
Main Authors: Wood, Mary H, Payagalage, Charanee Galabada, Geue, Thomas
Format: Article
Language:English
Subjects:
Adsorption
Animals
Cattle
Fibrinogen - chemistry
Hydrophobic and Hydrophilic Interactions
Neutron Diffraction
Quartz Crystal Microbalance Techniques
Serum Albumin, Bovine - chemistry
Sodium Dodecyl Sulfate - chemistry
Stainless Steel - chemistry
Surface Properties
Water - chemistry
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The binding of bovine serum albumin (BSA) to a 316L stainless steel surface from a buffer solution has been characterized using neutron reflectometry and quartz crystal microbalance measurements; coverage at all concentrations up to a near-physiological concentration was found to be relatively low (
ISSN:1520-6106
1520-5207
DOI:10.1021/acs.jpcb.8b01347