ArticleAngewandte Chemie (International ed. in English)2025
Diacylation of Peptides Enables the Construction of Functional Vesicles for Drug-Carrying Liposomes.
Article in Angewandte Chemie (International ed. in English), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- Self-Assembling Cationic Lipopeptides for the Construction of Functional Vesicular Gene-Delivery Systems.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Construction of Phospholipid-Like Vesicles by Aqueous Aminolysis of Acyl Thioesters With Diamino Acids.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
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Authors and funding
6 authors.
Funding
Abstract
Membrane-forming phospholipids are generated in cells by enzymatic diacylation of non-amphiphilic polar head groups. Analogous non-enzymatic processes may have been relevant at the origin of life and could have practical utility in membrane synthesis. However, aqueous head group diacylation is challenging in the absence of enzymes. The use of charged peptides instead of canonical phospholipid head groups offers advantages with respect to ease of acylation and chemical diversity. Here we demonstrate that native chemical ligation (NCL) enables in situ synthesis of diacylated lipopeptides (D-ALPs), which spontaneously self-assemble into micron-sized vesicles resembling cellular membranes. Diacylation occurs between non-amphiphilic peptides possessing an N-terminal cysteine, and acyl thioesters. Peptide head groups endow unique membrane functions, which is demonstrated by incorporation of an arginine-glycine-aspartic acid (RGD) motif, resulting in vesicle targeting to α
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