ArticleProceedings of the National Academy of Sciences of the United States of America2004
De novo design of conformationally flexible transmembrane peptides driving membrane fusion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 81 citations in OpenAlex.
- Conformational Flexibility of Transmembrane Helices: How it Works and Where it Matters.Chemical reviews · 2026Review
- Transmembrane domains of fusion proteins promote stalk formation by inducing membrane disorder.Biophysical journal · 2026Article
- Review
- Identification and Characteristics of Fusion Peptides Derived From Enveloped Viruses.Frontiers in chemistry · 2021Review
- Influenza A H1 and H3 Transmembrane Domains Interact Differently with Each Other and with Surrounding Membrane Lipids.Viruses · 2020Article
- Conformation and Trimer Association of the Transmembrane Domain of the Parainfluenza Virus Fusion Protein in Lipid Bilayers from Solid-State NMR: Insights into the Sequence Determinants of Trimer Structure and Fusion Activity.Journal of molecular biology · 2018Article
- Review
- A Central Small Amino Acid in the VAMP2 Transmembrane Domain Regulates the Fusion Pore in Exocytosis.Scientific reports · 2017Article
- Regulation of Exocytotic Fusion Pores by SNARE Protein Transmembrane Domains.Frontiers in molecular neuroscience · 2017Review
- The Multifaceted Role of SNARE Proteins in Membrane Fusion.Frontiers in physiology · 2017Review
- Viral fusion protein transmembrane domain adopts β-strand structure to facilitate membrane topological changes for virus-cell fusion.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Biologically active LIL proteins built with minimal chemical diversity.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Synaptobrevin Transmembrane Domain Dimerization Studied by Multiscale Molecular Dynamics Simulations.Biophysical journal · 2015Article
- Vacuolar SNARE protein transmembrane domains serve as nonspecific membrane anchors with unequal roles in lipid mixing.The Journal of biological chemistry · 2015Article
- Sequence-dependent backbone dynamics of a viral fusogen transmembrane helix.Protein science : a publication of the Protein Society · 2012Article
- Probing the lipid-protein interface using model transmembrane peptides with a covalently linked acyl chain.Biophysical journal · 2011Article
- Helix-destabilizing, beta-branched, and polar residues in the baboon reovirus p15 transmembrane domain influence the modularity of FAST proteins.Journal of virology · 2011Article
- Residue-specific side-chain packing determines the backbone dynamics of transmembrane model helices.Biophysical journal · 2010Article
- Direct visualization of large and protein-free hemifusion diaphragms.Biophysical journal · 2010Article
- A tail-anchored myotonic dystrophy protein kinase isoform induces perinuclear clustering of mitochondria, autophagy, and apoptosis.PloS one · 2009Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fusion of biological membranes is mediated by distinct integral membrane proteins, e.g., soluble N-ethylmaleimide-sensitive factor attachment protein receptors and viral fusion proteins. Previous work has indicated that the transmembrane segments (TMSs) of such integral membrane proteins play an important role in fusion. Furthermore, peptide mimics of the transmembrane part can drive the fusion of liposomes, and evidence had been obtained that fusogenicity depends on their conformational flexibility. To test this hypothesis, we present a series of unnatural TMSs that were designed de novo based on the structural properties of hydrophobic residues. We find that the fusogenicity of these peptides depends on the ratio of alpha-helix-promoting Leu and beta-sheet-promoting Val residues and is enhanced by helix-destabilizing Pro and Gly residues within their hydrophobic cores. The ability of these peptides to refold from an alpha-helical state to a beta-sheet conformation and backwards was determined under different conditions. Membrane fusogenic peptides with mixed Leu/Val sequences tend to switch more readily between different conformations than a nonfusogenic peptide with an oligo-Leu core. We propose that structural flexibility of these TMSs is a prerequisite of fusogenicity.
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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.