Stabilization of Neutral NH2-R-COOH Form of the Antihypertensive Peptides L-Valyl-L-Prolyl-L-Proline and L-Isoleucyl-L-Prolyl-L-Proline

Title: Stabilization of Neutral NH2-R-COOH Form of the Antihypertensive Peptides L-Valyl-L-Prolyl-L-Proline and L-Isoleucyl-L-Prolyl-L-Proline

Volume: 16 Issue: 2

Author(s): Tsonko Kolev, Bojidarka B. Koleva, Ivanka Stoineva, Boryana Jakimova and Bojidar Tchorbanov

Affiliation:

Keywords: Tripeptide, H-Val-Pro-Pro-OH, H-Ile-Pro-Pro-OH, angiotensin-I converting enzyme

Abstract: Spectroscopic and structural elucidation of the peptides L-Valyl-L-Prolyl-L-Proline (1) and L-Isoleucyl-L-Prolyl- L-Proline (2) are reported on the basis of experimental linear-polarized IR-spectroscopy in solid-state, 1H-NMR data and DFT. Curiously, the experimental data shown that both peptides stabilized in solution and in solid-state neutral H2N-RCOOH form. Conformational analysis made, shown two strong intramolecular NH2 … O=C-N(Amide) and O=C-OH … NH2 hydrogen bonds with lengths of 2.979 Å and 2.475 Å in (1) and 2.599 Å and 2.507 Å in (2) respectively. The presence of the Pro-Pro fold resulted to strong steric effect leading to the stabilization of free COOH and NH2 groups. The Erel values of zwitterion form are significant higher than the neutral forms with a difference of 1.2 and 0.9 kJ/mol. The manner of interaction of the peptides with angiotensin-I converting enzyme is proposed.

Cite this article as:

Kolev Tsonko, Koleva B. Bojidarka, Stoineva Ivanka, Jakimova Boryana and Tchorbanov Bojidar, Stabilization of Neutral NH2-R-COOH Form of the Antihypertensive Peptides L-Valyl-L-Prolyl-L-Proline and L-Isoleucyl-L-Prolyl-L-Proline, Protein & Peptide Letters 2009; 16 (2) . https://dx.doi.org/10.2174/092986609787316315

DOI https://dx.doi.org/10.2174/092986609787316315	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305