ArticleSmall (Weinheim an der Bergstrasse, Germany)2025
Self-Assembly of Off-Target Peptide Sequences: Implications for the Design of Soft Materials.
Article in Small (Weinheim an der Bergstrasse, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed.
- Structure-Function Regulation of Proteolytically Stable Amphiphilic Peptide-Based Soft Materials With Antimicrobial Efficacy Against Drug-Resistant Strains and Anticancer Activity in Triple-Negative Breast Cancer Cells.Chembiochem : a European journal of chemical biology · 2026Article
- Injectable dual-affinity self-assembling peptide hydrogels for local controlled delivery of therapeutic antibodies.Asian journal of pharmaceutical sciences · 2026Article
- Self-Assembly of Off-Target Peptide Sequences: Implications for the Design of Soft Materials.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
Abstract
The self-assembly of short peptides into defined nanostructures is one method for preparing soft materials and gels. Indeed, many useful materials can be prepared by the self-assembly of oligopeptides. The design rules around such peptides are relatively established, and they assume well-defined and pure materials. In many cases, however, the purity of the peptide is less than 95%, and the ability of likely impurities to self-assemble is an open question. Here, the self-assembly of the gel-forming octapeptide FEFEFKFK and two analogues, EFEFKFK and FEFEfKFK, is discussed to examine the effect of an amino acid deletion and of epimerization at one position. Both the truncated peptide and epimerized peptide can still form gels. Mixing these peptides with the parent FEFEFKFK leads to the formation of new, but different, self-assembled structures. This has direct implications for the understanding of the necessary design rules for self-assembly regarding the influence of potential impurity in these systems, as well as demonstrating that much remains to be learned about sequence to structure relationships in self-assembling peptide systems.
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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.