Evidence map›Paper›PMID 27144779›Full record

ArticleACS applied materials & interfaces2016

Competitive Adsorption of Plasma Proteins Using a Quartz Crystal Microbalance.

Helena P Felgueiras, N Sanjeeva Murthy, Sven D Sommerfeld, M Manuela Brás, Véronique Migonney, Joachim Kohn

Abstract read
In one paragraph

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.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
3.0field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 50 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 3 countries.

Helena P FelgueirasLaboratory of Biomaterials and Specialty Polymers, LBPS-CSPBAT CNRS UMR 7244, Institut Galilée, Université Paris 13 , 93430 Villetaneuse, France.
N Sanjeeva MurthyNew Jersey Center for Biomaterials, Rutgers University , 145 Bevier Road, Piscataway, New Jersey 08854, United States.
Sven D SommerfeldNew Jersey Center for Biomaterials, Rutgers University , 145 Bevier Road, Piscataway, New Jersey 08854, United States.
M Manuela BrásI3S - Institute for Innovation and Health, University of Porto , Rua Alfredo Allen 208, 4200-135 Porto, Portugal.
Véronique MigonneyLaboratory of Biomaterials and Specialty Polymers, LBPS-CSPBAT CNRS UMR 7244, Institut Galilée, Université Paris 13 , 93430 Villetaneuse, France.
Joachim KohnNew Jersey Center for Biomaterials, Rutgers University , 145 Bevier Road, Piscataway, New Jersey 08854, United States.
Rutgers, The State University of New Jersey · USChimie, Structures et Propriétés de Biomatériaux et d'Agents Thérapeutiquesi3S - Instituto de Investigação e Inovação em Saúde, Universidade do Porto · PT

Funding

RESBIO - the Technology Resource for Polymeric BiomaterialsP41EB001046 · NIBIB · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI KOHN, JOACHIM B. · 2003 to 2017
$17.0M
NIBIB NIH HHS P41 EB001046
6 · The paper itself

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.

Indexed as

Quartz Crystal Microbalance TechniquesAdsorptionBiocompatible MaterialsBlood ProteinsBone SubstitutesGoldPolystyrenesSerum Albumin, BovineSurface PropertiesBiocompatible MaterialsBlood ProteinsBone SubstitutesGoldPolystyrenesSerum Albumin, Bovinebovine serum albumincollagen type Icompetitive adsorptionfibronectinhydrophobic surfacespoly(NaSS) surfaces

Identifiers

PMID27144779
PMCPMC6707081
OpenAlexW2346068928

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.