ArticleJournal of molecular biology2007
Folding amphipathic helices into membranes: amphiphilicity trumps hydrophobicity.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 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
84 citing papers in PubMed.
- Article
- Structure and Membrane Interactions of Two Helices from Mycobacterium tuberculosis FtsL, One Transmembrane and One Amphipathic.Journal of the American Chemical Society · 2026Article
- The LOK C-terminus is an IBAR-like domain that facilitates membrane binding and ezrin colocalization.Biophysical journal · 2026Article
- ACP-EPC: an interpretable deep learning framework for anticancer peptide prediction utilizing pre-trained protein language model and multi-view feature extracting strategy.Molecular diversity · 2026Article
- Schistosome esophageal gland factor MEG-8.2 drives host cell lysis and interacts with host immune proteins.PLoS pathogens · 2026Article
- Antimycobacterial peptides as natural therapeutics for tuberculosis: mechanisms and structural features.Frontiers in antibiotics · 2026Review
- Antimicrobial Peptides of the Cathelicidin Family: Focus on LL-37 and Its Modifications.International journal of molecular sciences · 2025Review
- Design, Synthesis, and Biological Evaluation of New Analogs of Aurein 1.2 Containing Non-Proteinogenic Amino Acids.Molecules (Basel, Switzerland) · 2025Article
- Charge, Hydrophobicity, and Lipid Type Drive Antimicrobial Peptides' Unique Perturbation Ensembles.Biochemistry · 2025Article
- Improving the antimicrobial activity of RP9 peptide through theoretical and experimental investigation.Biochemistry and biophysics reports · 2025Article
- Discovery and engineering of a novel peptide, Temporin-WY2, with enhanced in vitro and in vivo efficacy against multi-drug resistant bacteria.Scientific reports · 2024Article
- A Critical Review of Short Antimicrobial Peptides from Scorpion Venoms, Their Physicochemical Attributes, and Potential for the Development of New Drugs.The Journal of membrane biology · 2024Review
- Optimization of antimicrobial peptides for the application against biocorrosive bacteria.Applied microbiology and biotechnology · 2023Article
- Disparate Regions of the Human Chemokine CXCL10 Exhibit Broad-Spectrum Antimicrobial Activity against Biodefense and Antibiotic-Resistant Bacterial Pathogens.ACS infectious diseases · 2023Article
- Article
- Important Roles and Potential Uses of Natural and Synthetic Antimicrobial Peptides (AMPs) in Oral Diseases: Cavity, Periodontal Disease, and Thrush.Journal of functional biomaterials · 2022Review
- Alternative Antibiotics in Dentistry: Antimicrobial Peptides.Pharmaceutics · 2022Review
- Biotherapeutic effect of cell-penetrating peptides against microbial agents: a review.Tissue barriers · 2022Review
- Article
- Article
24 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
High amphiphilicity is a hallmark of interfacial helices in membrane proteins and membrane-active peptides, such as toxins and antimicrobial peptides. Although there is general agreement that amphiphilicity is important for membrane-interface binding, an unanswered question is its importance relative to simple hydrophobicity-driven partitioning. We have examined this fundamental question using measurements of the interfacial partitioning of a family of 17-residue amidated-acetylated peptides into both neutral and anionic lipid vesicles. Composed only of Ala, Leu, and Gln residues, the amino acid sequences of the peptides were varied to change peptide amphiphilicity without changing total hydrophobicity. We found that peptide helicity in water and interface increased linearly with hydrophobic moment, as did the favorable peptide partitioning free energy. This observation provides simple tools for designing amphipathic helical peptides. Finally, our results show that helical amphiphilicity is far more important for interfacial binding than simple hydrophobicity.
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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.