Cyclotheonamides E2 and E3, new potent serine protease inhibitors from the marine sponge of the genus Theonella

Youichi Nakao, N. Oku, S. Matsunaga, N. Fusetani

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

Two new potent serine protease inhibitors, cyclotheonamides E2 (3) and E3 (4), have been isolated from a marine sponge of the genus Theonella. Their structures were determined by interpretation of spectral data and chemical degradation studies. They are closely related to the previously reported cyclotheonamide E, from which they differ in the N-acyl group of the alanyl side chain. Cyclotheonamides E, E2, and E3 were more active against thrombin than against trypsin.

Original languageEnglish
Pages (from-to)667-670
Number of pages4
JournalJournal of Natural Products
Volume61
Issue number5
DOIs
Publication statusPublished - 1998
Externally publishedYes

Fingerprint

Theonella
chemical degradation
Serine Proteinase Inhibitors
thrombin
Porifera
serine proteinases
proteinase inhibitors
spectral analysis
trypsin
Thrombin
Trypsin
Degradation
cyclotheonamide E
cyclotheonamide E3
cyclotheonamide E2

ASJC Scopus subject areas

  • Plant Science
  • Chemistry (miscellaneous)
  • Drug Discovery
  • Organic Chemistry
  • Pharmacology

Cite this

Cyclotheonamides E2 and E3, new potent serine protease inhibitors from the marine sponge of the genus Theonella. / Nakao, Youichi; Oku, N.; Matsunaga, S.; Fusetani, N.

In: Journal of Natural Products, Vol. 61, No. 5, 1998, p. 667-670.

Research output: Contribution to journalArticle

@article{da7466c7e6a14c7885494ab19c7027a5,
title = "Cyclotheonamides E2 and E3, new potent serine protease inhibitors from the marine sponge of the genus Theonella",
abstract = "Two new potent serine protease inhibitors, cyclotheonamides E2 (3) and E3 (4), have been isolated from a marine sponge of the genus Theonella. Their structures were determined by interpretation of spectral data and chemical degradation studies. They are closely related to the previously reported cyclotheonamide E, from which they differ in the N-acyl group of the alanyl side chain. Cyclotheonamides E, E2, and E3 were more active against thrombin than against trypsin.",
author = "Youichi Nakao and N. Oku and S. Matsunaga and N. Fusetani",
year = "1998",
doi = "10.1021/np970544n",
language = "English",
volume = "61",
pages = "667--670",
journal = "Journal of Natural Products",
issn = "0163-3864",
publisher = "American Chemical Society",
number = "5",

}

TY - JOUR

T1 - Cyclotheonamides E2 and E3, new potent serine protease inhibitors from the marine sponge of the genus Theonella

AU - Nakao, Youichi

AU - Oku, N.

AU - Matsunaga, S.

AU - Fusetani, N.

PY - 1998

Y1 - 1998

N2 - Two new potent serine protease inhibitors, cyclotheonamides E2 (3) and E3 (4), have been isolated from a marine sponge of the genus Theonella. Their structures were determined by interpretation of spectral data and chemical degradation studies. They are closely related to the previously reported cyclotheonamide E, from which they differ in the N-acyl group of the alanyl side chain. Cyclotheonamides E, E2, and E3 were more active against thrombin than against trypsin.

AB - Two new potent serine protease inhibitors, cyclotheonamides E2 (3) and E3 (4), have been isolated from a marine sponge of the genus Theonella. Their structures were determined by interpretation of spectral data and chemical degradation studies. They are closely related to the previously reported cyclotheonamide E, from which they differ in the N-acyl group of the alanyl side chain. Cyclotheonamides E, E2, and E3 were more active against thrombin than against trypsin.

UR - http://www.scopus.com/inward/record.url?scp=0031799026&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031799026&partnerID=8YFLogxK

U2 - 10.1021/np970544n

DO - 10.1021/np970544n

M3 - Article

VL - 61

SP - 667

EP - 670

JO - Journal of Natural Products

JF - Journal of Natural Products

SN - 0163-3864

IS - 5

ER -