ReviewBiochimica et biophysica acta2014
Peptide entry inhibitors of enveloped viruses: the importance of interfacial hydrophobicity.
Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
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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.
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Who cites it
81 citing papers in PubMed.
- Screening for Peptides to Bind and Functionally Inhibit SARS-CoV-2 Fusion Peptide Using Mirrored Combinatorial Phage Display and Human Proteomic Phage Display.Molecules (Basel, Switzerland) · 2026Article
- Inhibition of Chikungunya virus nsP2 protease in vitro by scorpion venom peptide pantinin-1.PloS one · 2026Article
- Structure-Guided Design of Peptide Inhibitors Targeting Class I Viral Fusion Proteins.Pathogens (Basel, Switzerland) · 2025Review
- Deoxyshikonin Inhibits Influenza A Virus Infection at an Early Stage.International journal of molecular sciences · 2025Article
- Deep learning in the discovery of antiviral peptides and peptidomimetics: databases and prediction tools.Molecular diversity · 2025Review
- A hybrid framework of generative deep learning for antiviral peptide discovery.Scientific reports · 2025Article
- Research strategies of the N-peptide fusion inhibitor: a promising direction for discovering novel antivirals.Journal of virology · 2025Review
- Antiviral strategies against influenza virus: an update on approved and innovative therapeutic approaches.Cellular and molecular life sciences : CMLS · 2025Review
- A Comprehensive Review of the Development and Therapeutic Use of Antivirals in Flavivirus Infection.Viruses · 2025Review
- Harnessing Antiviral Peptides: From Molecular Mechanisms to Clinical Translation.Current research in pharmacology and drug discovery · 2025Review
- Antiviral Activities of Mastoparan-L-Derived Peptides against Human Alphaherpesvirus 1.Viruses · 2024Article
- Impact of camel milk lactoferrin peptides against breast cancer cells:Frontiers in pharmacology · 2024Article
- Vector-Transmitted Flaviviruses: An Antiviral Molecules Overview.Microorganisms · 2023Review
- Prospecting native and analogous peptides with anti-SARS-CoV-2 potential derived from the trypsin inhibitor purified from tamarind seeds.Arabian journal of chemistry · 2023Article
- Inhibition of Cytomegalovirus byViruses · 2023Article
- Antiviral Approaches against Influenza Virus.Clinical microbiology reviews · 2023Review
- Antiviral activity of marine sulfated glycans against pathogenic human coronaviruses.Scientific reports · 2023Article
- Recent Patents and FDA-Approved Drugs Based on Antiviral Peptides and Other Peptide-Related Antivirals.International journal of peptide research and therapeutics · 2023Review
- SARS-CoV-2 and its new variants: a comprehensive review on nanotechnological application insights into potential approaches.Applied nanoscience · 2023Review
- Structural understanding of SARS-CoV-2 virus entry to host cells.Frontiers in molecular biosciences · 2023Review
21 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
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
There are many peptides known that inhibit the entry of enveloped viruses into cells, including one peptide that is successfully being used in the clinic as a drug. In this review, we discuss the discovery, antiviral activity and mechanism of action of such peptides. While peptide entry inhibitors have been discovered by a wide variety of approaches (structure-based, accidental, intentional, rational and brute force) we show here that they share a common physical chemical property: they are at least somewhat hydrophobic and/or amphipathic and have a propensity to interact with membrane interfaces. We propose that this propensity drives a shared mechanism of action for many peptide entry inhibitors, involving direct interactions with viral and cellular membranes, as well as interactions with the complex hydrophobic protein/lipid interfaces that are exposed, at least transiently, during virus-cell fusion. By interacting simultaneously with the membrane interfaces and other critical hydrophobic surfaces, we hypothesize that peptide entry inhibitors can act by changing the physical chemistry of the membranes, and the fusion protein interfaces bridging them, and by doing so interfere with the fusion of cellular and viral membranes. Based on this idea, we propose that an approach that focuses on the interfacial hydrophobicity of putative entry inhibitors could lead to the efficient discovery of novel, broad-spectrum viral entry inhibitors. This article is part of a Special Issue entitled: Interfacially Active Peptides and Proteins. Guest Editors: William C. Wimley and Kalina Hristova.
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