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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Linear-Polarized IR-Spectroscopic and Structural Elucidation of Glycyl-L-Phenylalanyl-Glycine Hydrochloride Monohydrate

Author(s): Bojidarka B. Koleva

Volume 15, Issue 3, 2008

Page: [309 - 313] Pages: 5

DOI: 10.2174/092986608783744162

Price: $65

Abstract

As a part of our spectroscopic and structural elucidation of small peptides, their salts and metal complexes, the polarized IR-spectroscopic and structural elucidation of the protonated form of glycyl-L-phenylalanyl-glycine as hydrochloride monohydrate (H-Gly-Phe-Gly-OHxHClxH2O) is reported. The obtained structure of the protonated tripeptide is supported by quantum chemical ab initio calculations at UHF level of theory and 6-31++G**, showing only one stable conformer with two intermolecular NH3 + … OH2 and (C=O)OH … OH2 hydrogen bonds. The Nterminus amide O=C-N-H amide fragment is flat trans-configured with a dihedral angle value of 179.0(7)°, while the corresponding group at Cterminus is with transoide-configurated and value of the dihedral angle of 151.1(3)°, respectively. In addition data of 1H- and 13C magnetic resonance spectroscopy (NMR), thermogravimetry (TGA), differential scanning calorimetry (DSC) and high performed liquid chromatography (HPLC) with tandem mass spectrometry (HPLC-MS/MS) as presented.

Keywords: Tripeptide, H-Gly-Phe-Gly-OH, salt, solid-state linear polarized IR-spectroscopy, quantum chemical calculations, 1H- and 13C NMR, HPLC MS/MS


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