ArticleBiomacromolecules2022
Design of Polypeptides Self-Assembling into Antifouling Coatings: Exploiting Multivalency.
Article in Biomacromolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Predicting Supramolecular Self-Assembly of Peptide Structures with AlphaFold3.bioRxiv : the preprint server for biology · 2026Article
- Bioorthogonal Mussel-Inspired Elastin-like Nanocoatings for Indwelling Devices.ACS applied materials & interfaces · 2025Article
- Nonfouling Coatings from Synthetic Intrinsically Disordered Proteins.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Contribution of the ELRs to the development of advancedFrontiers in bioengineering and biotechnology · 2024Review
- Modular Design for Proteins Assembling into Antifouling Coatings: Case of Gold Surfaces.Langmuir : the ACS journal of surfaces and colloids · 2023Article
- Spontaneous Self-Organized Order Emerging From Intrinsically Disordered Protein Polymers.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnologyReview
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We propose to exploit multivalent binding of solid-binding peptides (SBPs) for the physical attachment of antifouling polypeptide brushes on solid surfaces. Using a silica-binding peptide as a model SBP, we find that both tandem-repeated SBPs and SBPs repeated in branched architectures implemented via a multimerization domain work very well to improve the binding strength of polypeptide brushes, as compared to earlier designs with a single SBP. At the same time, for many of the designed sequences, either the solubility or the yield of recombinant production is low. For a single design, with the domain structure
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Registered trials
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.