ArticleACS applied materials & interfaces2016
Competitive Adsorption of Plasma Proteins Using a Quartz Crystal Microbalance.
Article in ACS applied materials & interfaces, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 50 citations in OpenAlex.
- Soft Interferometric Nanostrain Sensor Reveals Solid-Liquid Interfacial Tension Oscillation Amplified by Competitive Adsorption.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Self-assembly of short biopeptides onto skin tissue components studied using QCM-D.International journal of cosmetic science · 2025Article
- Unravelling Surface Modification Strategies for Preventing Medical Device-Induced Thrombosis.Advanced healthcare materials · 2024Review
- Practical Use of Quartz Crystal Microbalance Monitoring in Cartilage Tissue Engineering.Journal of functional biomaterials · 2022Review
- Titanium and Protein Adsorption: An Overview of Mechanisms and Effects of Surface Features.Materials (Basel, Switzerland) · 2021Review
- Spun Biotextiles in Tissue Engineering and Biomolecules Delivery Systems.Antibiotics (Basel, Switzerland) · 2020Review
- Grafting of architecture controlled poly(styrene sodium sulfonate) onto titanium surfaces using bio-adhesive molecules: Surface characterization and biological properties.Biointerphases · 2017Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
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.
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