Stability against enzymatic hydrolysis of endomorphin-1 analogues containing beta-proline.
The enantiomer of endomorphin-1 (Tyr-Pro-Trp-PheNH2) and the analogues containing (S)- or (R)-beta-proline have been synthesized, and their affinities towards mu-opioid receptors have been measured. As expected, the incubations of the different peptides with some commercially available enzymes showed that the presence of D-residues gave strong resistance towards digestion. The presence of beta-proline alone is sufficient to confer good resistance against the hydrolysis of the biologically strategic Pro-Trp bond.
Cardillo
Giuliana
G
Dipartimento di Chimica G. Ciamician, Università di Bologna, via Selmi 2, 40126 Bologna, Italy. cardillo@ciam.unibo.it
Gentilucci
Luca
L
Tolomelli
Alessandra
A
Calienni
Maria
M
Qasem
Ahmed R
AR
Spampinato
Santi
S
D000818:Animals; D018826:CD13 Antigens / Q000378:metabolism; D002268:Carboxypeptidases / Q000378:metabolism; D002918:Chymotrypsin / Q000378:metabolism; D006868:Hydrolysis; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism*; D011392:Proline / Q000737:chemistry*; D051381:Rats; D017450:Receptors, Opioid, mu / Q000819:agonists; D013237:Stereoisomerism; D014364:Tryptophan / Q000737:chemistry
D009842:Oligopeptides; D017450:Receptors, Opioid, mu; C105293:endomorphin 1; D014364:Tryptophan; D011392:Proline; D002268:Carboxypeptidases; D018826:CD13 Antigens; D002918:Chymotrypsin