ArticleNature communications2025
Direct detection of an NH-π hydrogen bond in an intrinsically disordered peptide.
Article in Nature communications, 2025. 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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Who cites it
3 citing papers in PubMed.
- Weak hydrogen bonding as the driver of aromatic hydration.Nature communications · 2026Article
- Special Issue "Application of NMR Spectroscopy in Biomolecules".International journal of molecular sciences · 2026Article
- Direct detection of an NH-π hydrogen bond in an intrinsically disordered peptide.Nature communications · 2025Article
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Authors and funding
13 authors.
Funding
Abstract
Hydrogen bonds play crucial roles in functional biomolecular dynamics. It is suggested that non-conventional hydrogen bonds engaging π electrons are prevalent in proteins. The experimental support for their existence is however limited. Here, we provide direct NMR spectroscopic evidence for the existence of an NH-π interaction in an intrinsically disordered peptide (E22G-Aβ40). In particular, we demonstrate the correlation between the amide proton of a glycine residue (Gly22) and the aromatic carbons of its preceding Phe20 through π hydrogen bond-mediated scalar coupling between them, as predicted by density functional theory calculations. Our results present a proof-of-principle example of NH-π interactions in an intrinsically disordered protein (IDP) and suggest the potential prevalence of π hydrogen bonds on the surface of IDPs. Direct experimental verification of NH-π interactions in folded proteins remains for future studies.
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