ArticleChemistry (Weinheim an der Bergstrasse, Germany)2020
Surface Design for Immobilization of an Antimicrobial Peptide Mimic for Efficient Anti-Biofouling.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 30 citations in OpenAlex.
- Peptide Photoimmobilization by Thiol-ene Chemistry for Enhanced Neural Cell Adhesion.ACS biomaterials science & engineering · 2025Article
- Medical Device-Associated Healthcare Infections: Sterilization and the Potential of Novel Biological Approaches to Ensure Patient Safety.International journal of molecular sciences · 2023Review
- Minimal Peptoid Dynamics Inform Self-Assembly Propensity.The journal of physical chemistry. B · 2023Article
- Bioinspired Polydopamine Coatings Facilitate Attachment of Antimicrobial Peptidomimetics with Broad-Spectrum Antibacterial Activity.International journal of molecular sciences · 2022Article
- Antibacterial and Antiviral Functional Materials: Chemistry and Biological Activity toward Tackling COVID-19-like Pandemics.ACS pharmacology & translational science · 2021Review
- Surface Design for Immobilization of an Antimicrobial Peptide Mimic for Efficient Anti-Biofouling.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Chain-End Modifications and Sequence Arrangements of Antimicrobial Peptoids for Mediating Activity and Nano-Assembly.Frontiers in chemistry · 2020Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
Abstract
Microbial surface attachment negatively impacts a wide range of devices from water purification membranes to biomedical implants. Mimics of antimicrobial peptides (AMPs) constituted from poly(N-substituted glycine) "peptoids" are of great interest as they resist proteolysis and can inhibit a wide spectrum of microbes. We investigate how terminal modification of a peptoid AMP-mimic and its surface immobilization affect antimicrobial activity. We also demonstrate a convenient surface modification strategy for enabling alkyne-azide "click" coupling on amino-functionalized surfaces. Our results verified that the N- and C-terminal peptoid structures are not required for antimicrobial activity. Moreover, our peptoid immobilization density and choice of PEG tether resulted in a "volumetric" spatial separation between AMPs that, compared to past studies, enabled the highest AMP surface activity relative to bacterial attachment. Our analysis suggests the importance of spatial flexibility for membrane activity and that AMP separation may be a controlling parameter for optimizing surface anti-biofouling.
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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.