ArticleBioconjugate chemistry2021
Peptide Amphiphilic-Based Supramolecular Structures with Anti-HIV-1 Activity.
Article in Bioconjugate chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed, 7 citations in OpenAlex.
- Antiviral Activity and Mucosal Safety of Novel Human-Milk-Inspired Antimicrobial Peptides.Pharmaceutics · 2026Article
- Self-Assembly of Anti-Inflammatory Peptide Amphiphiles for Mucosal Health.Chembiochem : a European journal of chemical biology · 2026Article
- Peptide Amphiphiles as Biodegradable Adjuvants for Efficient Retroviral Gene Delivery.Advanced healthcare materials · 2024Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In a previous work, we defined a novel HIV-1 fusion inhibitor peptide (E1P47) with a broad spectrum of activity against viruses from different clades, subtypes, and tropisms. With the aim to enhance its efficacy, in the present work we address the design and synthesis of several peptide amphiphiles (PAs) based on the E1P47 peptide sequence to target the lipid rafts of the cell membrane where the cell-cell fusion process takes place. We report the synthesis of novel PAs having a hydrophobic moiety covalently attached to the peptide sequence through a hydrophilic spacer of polyethylene glycol. Characterization of self-assembly in condensed phase and aqueous solution as well as their interaction with model membranes was analyzed by several biophysical methods. Our results demonstrated that the length of the spacer of polyethylene glycol, the position of the peptide conjugation as well as the type of the hydrophobic residue determine the antiviral activity of the construct. Peptide amphiphiles with one alkyl tail either in C-terminus (
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