ArticleThe journal of physical chemistry. B2019
Helical Structure of Recombinant Melittin.
Article in The journal of physical chemistry. B, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 35 citations in OpenAlex.
- Multidimensional Modification and Functional Optimization of Melittin: From Natural Toxic Peptide to Safe and Effective Therapeutics.Pharmaceutics · 2026Review
- Functional reprogramming of melittin by PluronicFrontiers in oncology · 2026Article
- Elucidating the Impact of Red Blood Cell Membrane Components on Melittin-Induced Pore Formation with Molecular Dynamics Simulations.The journal of physical chemistry. B · 2025Article
- Polyphenol-Mediated Peptide Assembly Modulates Melittin Toxicity: A Structure-Activity Strategy for Neutralizing the Interface Affinity of Pore-Forming Toxins to Cell Membranes.ACS applied materials & interfaces · 2025Article
- Review
- ANG-Modified Liposomes Coloaded With α-Melittin and Resveratrol Induce Apoptosis and Pyroptosis in Glioblastoma Cells by Impeding Wnt/β-Catenin Signaling.CNS neuroscience & therapeutics · 2025Article
- DIAPH1-MFN2 interaction regulates mitochondria-SR/ER contact and modulates ischemic/hypoxic stress.Nature communications · 2023Article
- Mechanistic Insight into the Early Stages of Toroidal Pore Formation by the Antimicrobial Peptide Smp24.Pharmaceutics · 2023Article
- An Updated Review Summarizing the Anticancer Efficacy of Melittin from Bee Venom in Several Models of Human Cancers.Nutrients · 2023Review
- Structures of calmodulin-melittin complexes show multiple binding modes lacking classical anchoring interactions.The Journal of biological chemistry · 2023Article
- Antimicrobial Peptides (AMPs): Potential Therapeutic Strategy against Trypanosomiases?Biomolecules · 2023Review
- Protein Based Biomaterials for Therapeutic and Diagnostic Applications.Progress in biomedical engineering (Bristol, England) · 2022Article
- Structure Analysis of Proteins and Peptides by Difference Circular Dichroism Spectroscopy.The protein journal · 2021Article
- Applications and evolution of melittin, the quintessential membrane active peptide.Biochemical pharmacology · 2021Review
- Article
- Investigation of the structure-activity relationship in ponericin L1 fromPeptide science (Hoboken, N.J.) · 2020Article
- Hydrophobic residues of melittin mediate its binding to αA-crystallin.Protein science : a publication of the Protein Society · 2020Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Melittin is an extensively studied, 26-residue toxic peptide from honey bee venom. Because of its versatility in adopting a variety of secondary (helix or coil) and quaternary (monomer or tetramer) structures in various environments, melittin has been the focus of numerous investigations as a model peptide in protein folding studies as well as in studies involving binding to proteins, lipids, and polysaccharides. A significant body of evidence supports the view that melittin binds to these macromolecules in a predominantly helical conformation, but detailed structural knowledge of this conformation is lacking. In this report, we present nuclear magnetic resonance (NMR)-based structural insights into the helix formation of recombinant melittin in the presence of trifluoroethanol (TFE): a known secondary structure inducer in peptides. These studies were performed at neutral pH, with micromolar amounts of the peptide. Using nuclear Overhauser effect (NOE)-derived distance restraints from three-dimensional NMR spectra, we determined the atomic resolution solution NMR structure of recombinant melittin bearing a TFE-stabilized helix. To circumvent the complications with structure determination of small peptides with high conformational flexibility, we developed a workflow for enhancing proton NOEs by increasing the viscosity of the medium. In the TFE-containing medium, recombinant monomeric melittin forms a long, continuous helical structure, which consists of the N- and C-terminal α-helices and the noncanonical 3
Indexed as
Identifiers
What OpenQuestion holds
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.