2 ISOMERIC ALPHA-ASPARTYL AND BETA-ASPARTYL DODECAPEPTIDES AND THEIR CYCLIC AMINO SUCCINYL ANALOG FROM THE AUSTRALIAN GREEN TREE FROG LITORIA-GILLENI

Authors
WAUGH RJ STEINBORNER ST BOWIE JH WALLACE JC TYLER MJ HU PF GROSS ML
Citation
Rj. Waugh et al., 2 ISOMERIC ALPHA-ASPARTYL AND BETA-ASPARTYL DODECAPEPTIDES AND THEIR CYCLIC AMINO SUCCINYL ANALOG FROM THE AUSTRALIAN GREEN TREE FROG LITORIA-GILLENI, Australian Journal of Chemistry, 48(12), 1995, pp. 1981-1987
Citations number
25
Categorie Soggetti
Chemistry
Journal title
Australian Journal of Chemistry → ACNP
ISSN journal
00049425
Volume
48
Issue
12
Year of publication
1995
Pages
1981 - 1987
Database
ISI
SICI code
0004-9425(1995)48:12<1981:2IAABD>2.0.ZU;2-6
Abstract
Three related peptides, caeridins 1.1-1.3, have been isolated from the green tree frog Litoria gilleni. Caeridins 1.1 and 1.2 are dodecapept ides differing only in having alpha and beta Asp at residue 4 [viz. Gl y Leu Leu Asp Gly Leu Leu Gly Thr Leu Gly Leu(NH2)]. Caeridin 1.3 is t he corresponding cyclic amino succinyl derivative derived formally by cyclization of Asp(4) and Gly(5). Hydrolysis of caeridin 1.3 yields ca eridin 1.1 and 1.2 in the ratio 3:1. This constitutes a rare case of t he isolation of three such related peptides from a natural system.