Stabilization of neutral NH2-R-COOH form of the antihypertensive peptides L-Valyl-L-Prolyl-L-Proline and L-Isoleucyl-L-Prolyl-L-Proline.
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-R-COOH 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 A and 2.475 A in (1) and 2.599 A and 2.507 A 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.
Kolev
Tsonko
T
Institute of Organic Chemistry, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria. Kolev@orgchm.bas.bg
Koleva
Bojidarka B
BB
Stoineva
Ivanka
I
Jakimova
Boryana
B
Tchorbanov
Bojidar
B
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry*; D000959:Antihypertensive Agents / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid; D007532:Isoleucine / Q000737:chemistry; D008958:Models, Molecular; D016011:Normal Distribution; D019906:Nuclear Magnetic Resonance, Biomolecular; D009842:Oligopeptides / Q000737:chemistry*; D011392:Proline / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared; D013057:Spectrum Analysis; D053719:Tandem Mass Spectrometry; D014633:Valine / Q000737:chemistry
D000806:Angiotensin-Converting Enzyme Inhibitors; D000959:Antihypertensive Agents; D009842:Oligopeptides; C489032:isoleucyl-prolyl-proline; D007532:Isoleucine; C489031:valyl-prolyl-proline; D011392:Proline; D014633:Valine