ArticleBiophysical journal2014
Water-peptide site-specific interactions: a structural study on the hydration of glutathione.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 49 citations in OpenAlex.
- Differences and Similarities in Protein and Nucleic Acid Structures and Their Biological Interactions.Current issues in molecular biology · 2025Review
- Review
- Trimethylamine-N-oxide depletes urea in a peptide solvation shell.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Visualization of Self-Assembly and Hydration of a β-Hairpin through Integrated Small and Wide-Angle Neutron Scattering.Biomacromolecules · 2023Article
- Structural Analysis of Molecular Materials Using the Pair Distribution Function.Chemical reviews · 2022Review
- Location and Conformation of the LKα14 Peptide in Water/Ethanol Mixtures.Langmuir : the ACS journal of surfaces and colloids · 2021Article
- Hydration of Carboxyl Groups: A Route toward Molecular Recognition?The journal of physical chemistry. B · 2020Article
- Nanostructured Coating for Biomaterial Lubrication through Biomacromolecular Recruitment.ACS applied materials & interfaces · 2020Article
- Protein Solvent Shell Structure Provides Rapid Analysis of Hydration Dynamics.Journal of chemical information and modeling · 2019Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Water-peptide interactions play an important role in determining peptide structure and function. Nevertheless, a microscopic description of these interactions is still incomplete. In this study we have investigated at the atomic scale length the interaction between water and the tripeptide glutathione. The rationale behind this work, based on the combination between a neutron diffraction experiment and a computer simulation, is twofold. It extends previous studies on amino acids, addressing issues such as the perturbation of the water network brought by a larger biomolecule in solution. In addition, and more importantly, it seeks a possible link between the atomic length scale description of the glutathione-water interaction with the specific biological functionality of glutathione, an important intracellular antioxidant. Results indicate a rather weak hydrogen bond between the thiol (-SH) group of cysteine and its first neighbor water molecule. This -SH group serves as a proton donor, is responsible for the biological activity of glutathione, and it is involved in the formation of glutathione disulfide, the oxidized form of glutathione. Moreover, the hydration shell of the chemically identical carboxylate group on the glutamic acid residue and on the glycine residue shows an intriguing different spatial location of water molecules and coordination numbers around the two CO2(-) groups.
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Registered trials
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