Life Sciences 1983-10-17

Analgesic properties of N-terminal substituted phenylalanyl-alanine.

G Borin, P Giusti, L Cima

Index: Life Sci. 33(16) , 1575-80, (1983)

Full Text: HTML

Abstract

Phenylalanylalanine, an in vitro inhibitor of enkephalinase, and some of its N alpha-derivatives are shown to possess an analgesic action when injected i.p. and i.c.v. into mice in the presence or absence of Leu5-enkephalin. In the second case a synergistic response is observed. The intensity of the analgesic response depends markedly on the nature of the N-terminal substituent which affects the hydrophobic character of the resulting dipeptide, its subsequent transport and probably its rate of biotransformation by cleaving enzymes.

Related Compounds

  • Phe-Ala

Related Articles:

Alkali metal complexes of the dipeptides PheAla and AlaPhe: IRMPD spectroscopy.

2008-03-14

[ChemPhysChem 9 , 579-589, (2008)]

Single-conformation ultraviolet and infrared spectroscopy of model synthetic foldamers: beta-peptides Ac-beta3-hPhe-beta3-hAla-NHMe and Ac-beta3-hAla-beta3-hPhe-NHMe.

2008-04-09

[J. Am. Chem. Soc. 130(14) , 4795-807, (2008)]

A novel inhibitor of the mammalian peptide transporter PEPT1.

2001-04-10

[Biochemistry 40(14) , 4454-8, (2001)]

P3 cap modified Phe*-Ala series BACE inhibitors.

2004-01-05

[Bioorg. Med. Chem. Lett. 14(1) , 245-50, (2004)]

Dipeptide transport characteristics of the apical membrane of rat lung type II pneumocytes.

1995-08-01

[Am. J. Physiol. 269(2 Pt 1) , L137-43, (1995)]

More Articles...