A series of "nonclassical" endogenous opioid peptides (hemorphins) have been identified in the course of the study of proteolytic fragments of bovine blood hemoglobin. Depending on the N-terminal sequences the sub-families of LVV-emorphins, VV-hemorphins, and V-hemorphins can be distinguished. It was shown that the overall activity varied considerably among different hemorphins which points to the importance of the N-terminal hydrophobic residues on structure-function relationship. It is well accepted that the binding of the ligand to its receptor is mediated by ion-ion interactions, hydrogen bonding, dipole-dipole interactions, lipophilicity, and shape complementarity but the relative contributions of each of these interactions is still poor understood. We pursued this goal by examination of the conformational and dynamic properties of synthetic analogues sequences carefully selected for their complementary biological properties. In this work it has been observed tetra- and penta-peptides fragments of N-terminal protected LVV-hemorphins which are well known to be opioid receptor ligands and immunoregulatory peptides in order to study the structural-functional peculiarity. Structural study in CHCl3 has been directed towards peptides with the follow aminoacidic sequence: Boc-Leu-Val-Val-OMe, Boc-Leu-Val-Val-Tyr-OMe, Boc-Leu-Val-Val-Phe-OMe, Boc-Leu-Val-Val-Tyr-Pro-OMe. These products have been synthesized, purified, and then analyzed by NMR spectroscopy, employing both mono- and bi- dimensional homo- and hetero- nuclear correlation 1H-1H, 1H-13C techniques through which it is possible to obtain structural and conformational informations. The result obtained are compared and discussed. References Fenude E., Dettori A., Demontis M.P., Alberico E., & al., Pharm. Res., 2003, 47, 53 Fenude E., Dedola S., Fais M., VII Convegno "Complex Systems: structure, properties, reactivity and dynamics, 2005, Alghero, 13-15 Giugno Fenude E., Roggio A.M., XXII Congresso Nazionale della Società Chimica
The Hemorphins: a new class of opioid peptides derived from Hemoglobin
Fenude Emma;
2015
Abstract
A series of "nonclassical" endogenous opioid peptides (hemorphins) have been identified in the course of the study of proteolytic fragments of bovine blood hemoglobin. Depending on the N-terminal sequences the sub-families of LVV-emorphins, VV-hemorphins, and V-hemorphins can be distinguished. It was shown that the overall activity varied considerably among different hemorphins which points to the importance of the N-terminal hydrophobic residues on structure-function relationship. It is well accepted that the binding of the ligand to its receptor is mediated by ion-ion interactions, hydrogen bonding, dipole-dipole interactions, lipophilicity, and shape complementarity but the relative contributions of each of these interactions is still poor understood. We pursued this goal by examination of the conformational and dynamic properties of synthetic analogues sequences carefully selected for their complementary biological properties. In this work it has been observed tetra- and penta-peptides fragments of N-terminal protected LVV-hemorphins which are well known to be opioid receptor ligands and immunoregulatory peptides in order to study the structural-functional peculiarity. Structural study in CHCl3 has been directed towards peptides with the follow aminoacidic sequence: Boc-Leu-Val-Val-OMe, Boc-Leu-Val-Val-Tyr-OMe, Boc-Leu-Val-Val-Phe-OMe, Boc-Leu-Val-Val-Tyr-Pro-OMe. These products have been synthesized, purified, and then analyzed by NMR spectroscopy, employing both mono- and bi- dimensional homo- and hetero- nuclear correlation 1H-1H, 1H-13C techniques through which it is possible to obtain structural and conformational informations. The result obtained are compared and discussed. References Fenude E., Dettori A., Demontis M.P., Alberico E., & al., Pharm. Res., 2003, 47, 53 Fenude E., Dedola S., Fais M., VII Convegno "Complex Systems: structure, properties, reactivity and dynamics, 2005, Alghero, 13-15 Giugno Fenude E., Roggio A.M., XXII Congresso Nazionale della Società ChimicaI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
