ArticleJournal of medicinal chemistry2012
From a marine neuropeptide to antimicrobial pseudopeptides containing aza-β(3)-amino acids: structure and activity.
Article in Journal of medicinal chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 29 citations in OpenAlex.
- Advances in Peptidomimetics for Next-Generation Therapeutics: Strategies, Modifications, and Applications.Chemical reviews · 2025Review
- OctoPartenopin: Identification and Preliminary Characterization of a Novel Antimicrobial Peptide from the Suckers ofMarine drugs · 2020Article
- Novel antibiotics effective against gram-positive and -negative multi-resistant bacteria with limited resistance.PLoS biology · 2019Article
- Consecutive hydrazino-Ugi-azide reactions: synthesis of acylhydrazines bearing 1,5-disubstituted tetrazoles.Beilstein journal of organic chemistry · 2017Article
- Synthesis of acylhydrazino-peptomers, a new class of peptidomimetics, by consecutive Ugi and hydrazino-Ugi reactions.Beilstein journal of organic chemistry · 2016Article
- Synthesis of hybrid hydrazino peptides: protected vs unprotected chiral α-hydrazino acids.SpringerPlus · 2015Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Incorporation of aza-β(3)-amino acids into an endogenous neuropeptide from mollusks (ALSGDAFLRF-NH(2)) with weak antimicrobial activity allows the design of new AMPs sequences. Depending on the nature of the substitution, this can render the pseudopeptides inactive or lead to a drastic enhancement of the antimicrobial activity without high cytotoxicity. Structural studies of the pseudopeptides carried out by NMR and circular dichroism show the impact of aza-β(3)-amino acids on peptide structure. The first three-dimensional structures of pseudopeptides containing aza-β(3)-amino acids in aqueous micellar SDS were determined and demonstrate that the hydrazino turn can be formed in aqueous solution. Thus, AMP activity can be modulated through structural modifications induced by the nature and the position of such amino acid analogues in the peptide sequences.
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Registered trials
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