Evidence map›Paper›PMID 32268265›Full record

ReviewColloids and surfaces. B, Biointerfaces2020

Fundamental Principles of the Thermodynamics and Kinetics of Protein Adsorption to Material Surfaces.

Robert A Latour

Abstract readReview
In one paragraph

Review in Colloids and surfaces. B, Biointerfaces, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
–field-weighted citation impact
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

41 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Investigating the Effects of Nanogels in Promoting Protein Crystallization.International journal of molecular sciences · 2026
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Study of the Reaction Mechanism of the Excessive Adsorption of MnInternational journal of molecular sciences · 2025
    Article
  19. Plasmonic Single-Molecule Affinity Detection at 10Advanced materials (Deerfield Beach, Fla.) · 2025
    Article
  20. Article
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

1 author.

Robert A LatourMcQueen-Quattlebaum Professor Department of Bioengineering, Clemson University, Clemson, SC, United States. Electronic address: LatourR@clemson.edu.

Funding

Surface Analysis Facility for Biomedical ProblemsP41EB002027 · NIBIB · UNIVERSITY OF WASHINGTON · PI CASTNER, DAVID G · 2003 to 2019
$17.6M
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
Targeted Nano-therapeutics for Neural RegenerationP20GM103444 · NIGMS · CLEMSON UNIVERSITY · PI MARKWALD, ROGER R, VYAVAHARE, NAREN R · 2012 to 2018
$14.9M
Transnational Research Imaging Core (TRI)P30GM131959 · NIGMS · CLEMSON UNIVERSITY · PI VYAVAHARE, NAREN R · 2019 to 2023
$5.9M
Nanoscale Investigation of Protein-Surface InteractionsR01GM074511 · NIGMS · UNIVERSITY OF WASHINGTON · PI CASTNER, DAVID G · 2006 to 2009
$2.3M
Force Field Development for Protein Absorption ModelingR01EB006163 · NIBIB · CLEMSON UNIVERSITY · PI LATOUR, ROBERT A · 2006 to 2009
$1.4M
NIBIB NIH HHS P41 EB001046NIBIB NIH HHS P41 EB002027NIBIB NIH HHS R01 EB006163NIGMS NIH HHS P20 GM103444NIGMS NIH HHS P30 GM131959NIGMS NIH HHS R01 GM074511
6 · The paper itself

Abstract

Protein adsorption is important for essentially any process that involves the contact of a protein-containing solution and a material surface, with the resulting formation of the adsorbed layer of protein determined by the thermodynamics and kinetics of the system involved. This paper presents an overview of the fundamentals of these processes. First, the hierarchical structure of proteins and the types of bonding that stabilize a protein's native-state structure are presented. This section is then followed by a section presenting the thermodynamic driving forces that influence the way that proteins adsorb and conformationally change for three characteristically different types of surface chemistries: nonpolar (hydrophobic) surfaces, neutral hydrophilic surfaces, and charged surfaces. The final section of this paper addresses how kinetics and thermodynamics combine together to influence protein adsorption behavior, followed by concluding remarks.

Indexed as

Hydrophobic and Hydrophilic InteractionsThermodynamicsAdsorptionAnimalsHumansKineticsProteinsSurface PropertiesProteinsKineticsProtein adsorptionThermodynamics

Identifiers

PMID32268265
PMCPMC7247955

What OpenQuestion holds

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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.