Literature DB >> 27144779

Competitive Adsorption of Plasma Proteins Using a Quartz Crystal Microbalance.

Helena P Felgueiras1, N Sanjeeva Murthy2, Sven D Sommerfeld2, M Manuela Brás3,4, Véronique Migonney1, Joachim Kohn2.   

Abstract

Proteins that get adsorbed onto the surfaces of biomaterials immediately upon their implantation mediate the interactions between the material and the environment. This process, in which proteins in a complex mixture compete for adsorption sites on the surface, is determined by the physicochemical interactions at the interface. Competitive adsorption of bovine serum albumin (BSA), fibronectin (Fn), and collagen type I (Col I), sequentially and from mixtures, was investigated so as to understand the performances of different surfaces used in biomedical applications. A quartz crystal microbalance with dissipation was used to monitor the adsorption of these proteins onto two materials used in functional bone replacement, a titanium alloy (Ti6Al4V) and Ti6Al4V physisorbed with poly(sodium styrenesulfonate) [poly(NaSS)], and three controls, gold, poly(desaminotyrosyltyrosine ethyl ester carbonate) [poly(DTEc)], and polystyrene (PS). In experiments with individual proteins, the adsorption was the highest with Fn and Col I and the least with BSA. Also, protein adsorption was the highest on poly(NaSS) and Ti6Al4V and the least on poly(DTEc). In sequential adsorption experiments, protein exchange was observed in BSA + Fn, Fn + Col I, and BSA + Col I sequences but not in Fn + BSA and Col I + BSA because of the lower affinity of BSA to surfaces relative to Fn and Col I. Protein adsorption was the highest with Col I + Fn on hydrophobic surfaces. In experiments with protein mixtures, with BSA & Fn, Fn appears to be preferentially adsorbed; with Fn & Col I, both proteins were adsorbed, probably as multilayers; and with Col I & BSA, the total amount of protein was the highest, greater than that in sequential and individual adsorption of the two proteins, probably because of the formation of BSA and Col I complexes. Protein conformational changes induced by the adsorbing surfaces, protein-protein interactions, and affinities of proteins appear to be the important factors that govern competitive adsorption. The findings reported here will be useful in understanding the host response to surfaces used for implants.

Entities:  

Keywords:  bovine serum albumin; collagen type I; competitive adsorption; fibronectin; hydrophobic surfaces; poly(NaSS) surfaces

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Year:  2016        PMID: 27144779      PMCID: PMC6707081          DOI: 10.1021/acsami.5b12600

Source DB:  PubMed          Journal:  ACS Appl Mater Interfaces        ISSN: 1944-8244            Impact factor:   9.229


  3 in total

1.  Grafting of architecture controlled poly(styrene sodium sulfonate) onto titanium surfaces using bio-adhesive molecules: Surface characterization and biological properties.

Authors:  Hamza Chouirfa; Margaret D M Evans; David G Castner; Penny Bean; Dimitri Mercier; Anouk Galtayries; Céline Falentin-Daudré; Véronique Migonney
Journal:  Biointerphases       Date:  2017-06-14       Impact factor: 2.456

Review 2.  Spun Biotextiles in Tissue Engineering and Biomolecules Delivery Systems.

Authors:  Catarina S Miranda; Ana R M Ribeiro; Natália C Homem; Helena P Felgueiras
Journal:  Antibiotics (Basel)       Date:  2020-04-12

Review 3.  Titanium and Protein Adsorption: An Overview of Mechanisms and Effects of Surface Features.

Authors:  Jacopo Barberi; Silvia Spriano
Journal:  Materials (Basel)       Date:  2021-03-24       Impact factor: 3.623

  3 in total

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