On the hydration structure of the pro-drug GPG-NH2 and its derivatives

Smith, Paul, Steinke, Nicola, Turner, John F C, McLain, Sylvia E and Lorenz, Christina D (2018) On the hydration structure of the pro-drug GPG-NH2 and its derivatives. Chemical Physics Letters, 706. pp. 228-236. ISSN 0009-2614

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Abstract

Molecular 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.

Item Type: Article
Keywords: molecular dynamics, prodrug, conformation, fluorine, molecular modeling
Schools and Departments: School of Life Sciences > Chemistry
Subjects: Q Science > QD Chemistry > QD0450 Physical and theoretical chemistry
Q Science > QD Chemistry > QD0450 Physical and theoretical chemistry > QD0474 Complex compounds (including clathrate and coordination compounds, chelates, and hydrates)
Depositing User: John Turner
Date Deposited: 15 Jun 2018 14:32
Last Modified: 02 Jul 2019 15:30
URI: http://sro.sussex.ac.uk/id/eprint/76551

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