Albumin adsorption on CoCrMo alloy surfaces

• Published in: Scientific reports Vol. 5; no. 1; p. 18403
• Main Authors: Yan, Yu, Yang, Hongjuan, Su, Yanjing, Qiao, Lijie
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 17.12.2015; Nature Publishing Group
• Subjects: 639/166/988; 639/301/54/1754; Adsorption; Alloys; Animals; Bovine serum albumin; Cattle; Chromium Alloys - chemistry; Cobalt - chemistry; Corrosion; Electrochemical Techniques - methods; Electrostatic properties; Humanities and Social Sciences; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Hydrophobicity; Isoelectric Point; Microscopy, Atomic Force - methods; Molybdenum - chemistry; multidisciplinary; pH effects; Science; Serum Albumin, Bovine - chemistry; Static Electricity
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/srep18403

Proteins can adsorb on the surface of artificial joints immediately after being implanted. Although research studying protein adsorption on medical material surfaces has been carried out, the mechanism of the proteins’ adsorption which affects the corrosion behaviour of such materials still lacks in situ observation at the micro level. The adsorption of bovine serum albumin (BSA) on CoCrMo alloy surfaces was studied in situ by AFM and SKPFM as a function of pH and the charge of CoCrMo alloy surfaces. Results showed that when the specimens were uncharged, hydrophobic interaction could govern the process of the adsorption rather than electrostatic interaction and BSA molecules tended to adsorb on the surfaces forming a monolayer in the side-on model. Results also showed that adsorbed BSA molecules could promote the corrosion process for CoCrMo alloys. When the surface was positively charged, the electrostatic interaction played a leading role in the adsorption process. The maximum adsorption occurred at the isoelectric point (pH 4.7) of BSA.