Evidence map›Paper›PMID 11535805›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

History dependence of protein adsorption kinetics.

C Calonder, Y Tie, P R Van Tassel

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

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  12. Quantifying nisin adsorption behavior at pendant PEO layers.Journal of colloid and interface science · 2013
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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

3 authors.

C CalonderDepartment of Chemical Engineering and Materials Science, Wayne State University, Detroit, MI 48202, USA.
Y Tie
P R Van Tassel

Funding

AFFINITY AND ELECTRIC FIELD TECHNIQUES FOR BIOMATERIALR01GM059487 · NIGMS · WAYNE STATE UNIVERSITY · PI VAN TASSEL, PAUL R · 1999 to 2001
$292k
NIGMS NIH HHS R01-GM59487
6 · The paper itself

Abstract

The behavior of proteins at biological and synthetic interfaces is often characterized by a strong history dependence caused by long relaxation times or irreversible transitions. In this work, we introduce the rate of adsorption as a means to systematically quantify the extent, and identify the underlying causes, of history dependence. We use multistep kinetic experiments in which the i'th step is an exposure of a Si(Ti)O(2) surface to a flowing fibronectin or cytochrome c solution of concentration c(i) for a time t(i) (c(i) = 0 corresponds to a rinse) and measure the protein adsorption by optical waveguide light mode spectroscopy. The rate of adsorption is sensitive to the structure of the adsorbed layer, and we observe it to greatly increase, for a given adsorbed density, when going from a first to a subsequent adsorption step. This increase is most pronounced when the duration of the initial adsorption step is long. We attribute these observations to the gradual and irreversible formation of protein clusters or locally ordered structures and use them to explain previous underestimates of kinetic data by mesoscopic model descriptions. A thorough understanding of these complex postadsorption events, and their impact on history dependence, is essential for many physiological and biotechnological processes. Optical waveguide lightmode spectroscopy is a promising technique for their macroscopic quantification.

Indexed as

AbsorptionCytochrome c GroupFibronectinsKineticsProteinsSilicon DioxideTitaniumCytochrome c GroupFibronectinsProteinsSilicon Dioxidesilicon titanium dioxideTitanium

Identifiers

PMID11535805
PMCPMC58523

What OpenQuestion holds

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Registered trials

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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.