TAILIEUCHUNG - Báo cáo khoa học: Comparison of the solution structures of angiotensin I & II Implication for structure-function relationship

Conformational analysis of angiotensin I (AI) and II (AII) peptides has been performed through 2D 1 H-NMRspectro-scopy in dimethylsulfoxide and 2,2,2-trifluoroethanol/H2 O. The solution structural models of AI and AII have been determined in dimethylsulfoxide using NOE distance and 3 JHNHacoupling constants. Finally, theAI family of models resulting from restrained energy minimization (REM) refinement, exhibits pairwise rmsd values for the family ensemble ± A ˚, ± A ˚, for backbone and heavy atoms, respectively, and the distance penalty function is calculated at ± A ˚ 2 . . | Eur. J. Biochem. 270 2163-2173 2003 FEBS 2003 doi Comparison of the solution structures of angiotensin I II Implication for structure-function relationship Georgios A. Spyroulias1 Panagiota Nikolakopoulou1 Andreas Tzakos3 loannis P. Gerothanassis3 Vassiliki Magafa1 Evy Manessi-Zoupa2 and Paul Cordopatis1 1 Departments of Pharmacy and 2Chemistry University of Patras Greece 3Department of Chemistry University of Ioannina Greece Conformational analysis of angiotensin I AI and II AII peptides has been performed through 2D 1H-NMR spectroscopy in dimethylsulfoxide and 2 2 2-trifluoroethanol H2O. The solution structural models of AI and AII have been determined in dimethylsulfoxide using NOE distance and 3JHNHa coupling constants. Finally the AI family of models resulting from restrained energy minimization REM refinement exhibits pairwise rmsd values for the family ensemble A A for backbone and heavy atoms respectively and the distance penalty function is calculated at A2. Comparable results have been afforded for AII ensemble rmsd values A A for backbone and heavy atoms respectively distance penalty function is A2 . The two peptides demonstrate similar N-terminal and different C-terminal conformation as a consequence of the presence absence of the His9-Leu10 dipeptide which plays an important role in the different biological function of the two peptides. Other conformational variations focused on the side-chain orientation of aromatic residues which constitute a biologically relevant hydrophobic core and whose inter-residue contacts are strong in dimethylsulfoxide and are retained even in mixed organic-aqueous media. Detailed analysis of the peptide structural features attempts to elucidate the conformational role of the C-terminal dipeptide to the different binding affinity of AI and AII towards the AT1 receptor and sets the basis for understanding the factors that might .

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