Following the characterization of callipeltin A (I) two new cytotoxic peptides, callipeltin A (II) and C (III), were isolated from the New Caledonian sponge Callipelta sp. Callipeltin B possess the same cyclic depsipeptidal structure as in callipeltin A and differs from I by having the N-terminal 2,3-dimethylpyroglutamic acid unit instead of the tripeptide chain with the N-terminus blocked by an hydroxyacid. Callipeltin C is simply the acyclic callipeltin A. The structures II-III have been detd. by NMR expts., FAB mass spectrometry, evaluation of the amino acids obtained by acid hydrolysis and by comparison of the data with those of callipeltin A.
Callipeltins B and C; bioactive peptides from a marine Lithistida sponge Callipelta sp / D'Auria, MARIA VALERIA; Zampella, Angela; Gomez Paloma, L.; Minale, L.; Debitus, C.; Roussakis, C.; Le Bert, V.. - In: TETRAHEDRON. - ISSN 0040-4020. - STAMPA. - 52:28(1996), pp. 9589-9596. [10.1016/0040-4020(96)00496-6]
Callipeltins B and C; bioactive peptides from a marine Lithistida sponge Callipelta sp
D'AURIA, MARIA VALERIA;ZAMPELLA, ANGELA;
1996
Abstract
Following the characterization of callipeltin A (I) two new cytotoxic peptides, callipeltin A (II) and C (III), were isolated from the New Caledonian sponge Callipelta sp. Callipeltin B possess the same cyclic depsipeptidal structure as in callipeltin A and differs from I by having the N-terminal 2,3-dimethylpyroglutamic acid unit instead of the tripeptide chain with the N-terminus blocked by an hydroxyacid. Callipeltin C is simply the acyclic callipeltin A. The structures II-III have been detd. by NMR expts., FAB mass spectrometry, evaluation of the amino acids obtained by acid hydrolysis and by comparison of the data with those of callipeltin A.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
