The opioid agonists endomorphins (TyreProeTrpePheeNH2; EM1 and TyreProePheePheeNH2; EM2) and morphiceptin (TyreProePheeProeNH2) exhibit an extremely high selectivity for m-opioid receptor. Here a series of novel EM2 and morphiceptin analogues containing in place of the proline at position 2 the S and R residues of b-homologues of proline (HPro), of 2-pyrrolidinemethanesulphonic acid (HPrs) and of 3-pyrrolidinesulphonic acid (bPrs) have been synthesized and their binding affinity and functional activity have been investigated. The highest m-receptor affinity is shown by [(S)bPrs2]EM2 analogue (6e) which represents the first example of a b-sulphonamido analogue in the field of opioid peptides.
Synthesis and activity of endomorphin-2 and morphiceptin analogues with proline surrogates in position 2.
Annalisa Masi;
2010
Abstract
The opioid agonists endomorphins (TyreProeTrpePheeNH2; EM1 and TyreProePheePheeNH2; EM2) and morphiceptin (TyreProePheeProeNH2) exhibit an extremely high selectivity for m-opioid receptor. Here a series of novel EM2 and morphiceptin analogues containing in place of the proline at position 2 the S and R residues of b-homologues of proline (HPro), of 2-pyrrolidinemethanesulphonic acid (HPrs) and of 3-pyrrolidinesulphonic acid (bPrs) have been synthesized and their binding affinity and functional activity have been investigated. The highest m-receptor affinity is shown by [(S)bPrs2]EM2 analogue (6e) which represents the first example of a b-sulphonamido analogue in the field of opioid peptides.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
