ArticleJournal of peptide science : an official publication of the European Peptide Society2021
Capacity for increased surface area in the hydrophobic core of β-sheet peptide bilayer nanoribbons.
Article in Journal of peptide science : an official publication of the European Peptide Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed.
- Comparison of Pleated and Rippled β-Sheet Assembly of Sequence Isomers of an Amphipathic Self-Assembling Peptide.Biochemistry · 2026Article
- Self-Assembly and Electrical Conductivity of a New [1]benzothieno[3,2-b][1]-benzothiophene (BTBT)-Peptide Hydrogel.Molecules (Basel, Switzerland) · 2023Article
- Novel Vaccine Strategies and Factors to Consider in Addressing Health Disparities of HPV Infection and Cervical Cancer Development among Native American Women.Medical sciences (Basel, Switzerland) · 2022Review
- Anti-Colonization Effect of Au Surfaces with Self-Assembled Molecular Monolayers Functionalized with Antimicrobial Peptides onAntibiotics (Basel, Switzerland) · 2021Article
- Capacity for increased surface area in the hydrophobic core of β-sheet peptide bilayer nanoribbons.Journal of peptide science : an official publication of the European Peptide Society · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Amphipathic peptides with amino acids arranged in alternating patterns of hydrophobic and hydrophilic residues efficiently self-assemble into β-sheet bilayer nanoribbons. Hydrophobic side chain functionality is effectively buried in the interior of the putative bilayer of these nanoribbons. This study investigates consequences on self-assembly of increasing the surface area of aromatic side chain groups that reside in the hydrophobic core of nanoribbons derived from Ac-(XKXE)
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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.