Direct detection of an NH-π hydrogen bond in an intrinsically disordered peptide

Luigi Russo, Dipendu Dhar, Robin Backer, Om Prakash, Fatima Matroodi, Kerstin Overkamp, Karin Giller, Stefan Becker, Christian Griesinger, Dieter Willbold, Barbara Rossi, Mehdi D. Davari () and Nasrollah Rezaei-Ghaleh ()
Additional contact information
Luigi Russo: University of Campania-Luigi Vanvitelli, Department of Environmental, Biological and Pharmaceutical Science and Technology
Dipendu Dhar: Leibniz Institute of Plant Biochemistry, Department of Bioorganic Chemistry
Robin Backer: Institute of Physical Biology, Heinrich Heine University (HHU) Düsseldorf
Om Prakash: University of Pavia, Department of Physics
Fatima Matroodi: Elettra Sincrotrone Trieste
Kerstin Overkamp: Max Planck Institute for Multidisciplinary Sciences, Department of NMR-based Structural Biology
Karin Giller: Max Planck Institute for Multidisciplinary Sciences, Department of NMR-based Structural Biology
Stefan Becker: Max Planck Institute for Multidisciplinary Sciences, Department of NMR-based Structural Biology
Christian Griesinger: Max Planck Institute for Multidisciplinary Sciences, Department of NMR-based Structural Biology
Dieter Willbold: Institute of Physical Biology, Heinrich Heine University (HHU) Düsseldorf
Barbara Rossi: Elettra Sincrotrone Trieste
Mehdi D. Davari: Leibniz Institute of Plant Biochemistry, Department of Bioorganic Chemistry
Nasrollah Rezaei-Ghaleh: Institute of Physical Biology, Heinrich Heine University (HHU) Düsseldorf

Nature Communications, 2025, vol. 16, issue 1, 1-11

Abstract: 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.

Date: 2025
References: View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-025-66013-2 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-66013-2

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-025-66013-2

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().