On_the_hydration_structure_SMITH_Accepted27May2018_GREEN_AAM.pdf (8.79 MB)
On the hydration structure of the pro-drug GPG-NH2 and its derivatives
journal contribution
posted on 2023-06-09, 13:48 authored by Paul Smith, Nicola Steinke, John TurnerJohn Turner, Sylvia E McLain, Christina D LorenzMolecular dynamics simulations were used to investigate the hydration and structure of the tripeptide GPG-NH2, and the effect of substituting a fluorine or hydroxyl group onto one of the Ca positions in the glycinamide portion of the molecule. The fluorinated and hydroxylated peptides both display a slight dehydration of the proline and glycinamide residues and a different conformation of the glycinamide residue backbone than the GPG peptide. These two effects result in a significant decrease in the water-mediated interactions between the Gly1 and glycinamide residues, which had previously been shown to nucleate beta turns in GPG-NH2.
History
Publication status
- Published
File Version
- Accepted version
Journal
Chemical Physics LettersISSN
0009-2614Publisher
ElsevierExternal DOI
Volume
706Page range
228-236Department affiliated with
- Chemistry Publications
Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2018-06-15First Open Access (FOA) Date
2021-04-30First Compliant Deposit (FCD) Date
2018-06-14Usage metrics
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