Evidence map›Paper›PMID 30966458›Full record

ArticlePolymers2018

KnowVolution of the Polymer-Binding Peptide LCI for Improved Polypropylene Binding.

Kristin Rübsam, Mehdi D Davari, Felix Jakob, Ulrich Schwaneberg

Open access · goldAbstract read
In one paragraph

Article in Polymers, 2018. 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
2.3field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 67 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

4 authors at 2 institutions in 1 country.

Kristin RübsamInstitute of Biotechnology, RWTH Aachen University, Worringerweg 3, D-52074 Aachen, Germany. k.ruebsam@biotec.rwth-aachen.de.
Mehdi D DavariInstitute of Biotechnology, RWTH Aachen University, Worringerweg 3, D-52074 Aachen, Germany. m.davari@biotec.rwth-aachen.de.
Felix JakobDWI-Leibniz-Institute for Interactive Materials, Forckenbeckstrasse 50, D-52074 Aachen, Germany. jakob@dwi.rwth-aachen.de.
Ulrich SchwanebergInstitute of Biotechnology, RWTH Aachen University, Worringerweg 3, D-52074 Aachen, Germany. u.schwaneberg@biotec.rwth-aachen.de.
RWTH Aachen University · DEDWI – Leibniz Institute for Interactive Materials · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The functionalization of polymer surfaces by polymer-binding peptides offers tremendous opportunities for directed immobilization of enzymes, bioactive peptides, and antigens. The application of polymer-binding peptides as adhesion promoters requires reliable and stable binding under process conditions. Molecular modes of interactions between material surfaces, peptides, and solvent are often not understood to an extent that enables (semi-) rational design of polymer-binding peptides, hindering the full exploitation of their potential. Knowledge-gaining directed evolution (KnowVolution) is an efficient protein engineering strategy that facilitates tailoring protein properties to application demands through a combination of directed evolution and computational guided protein design. A single round of KnowVolution was performed to gain molecular insights into liquid chromatography peak I peptide, 47 aa (LCI)-binding to polypropylene (PP) in the presence of the competing surfactant Triton X-100. KnowVolution yielded a total of 8 key positions (D19, S27, Y29, D31, G35, I40, E42, and D45), which govern PP-binding in the presence of Triton X-100. The recombination of two of the identified amino acid substitutions (Y29R and G35R; variant KR-2) yielded a 5.4 ± 0.5-fold stronger PP-binding peptide compared to LCI WT in the presence of Triton X-100 (1 mM). The LCI variant KR-2 shows a maximum binding capacity of 8.8 ± 0.1 pmol/cm² on PP in the presence of Triton X-100 (up to 1 mM). The KnowVolution approach enables the development of polymer-binding peptides, which efficiently coat and functionalize PP surfaces and withstand surfactant concentrations that are commonly used, such as in household detergents.

Indexed as

anchor peptidesdirected evolutionimmobilizationpolymer-binding peptidessurface functionalization

Identifiers

PMID30966458
PMCPMC6415234
OpenAlexW2798145671

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.