Axinellin C, a proline-rich cyclic octapeptide isolated from the Fijian marine sponge Stylotella aurantium

Jioji Natadra Tabudravu, L. A. Morris, J. J. Kettenes-van den Bosch, Marcel Jaspars

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

The structure of a new cyclic octapeptide, axinellin C, (cyclo[Thr(1)-Val(2)-Pro(3)-Trp(4)-Pro(5)-Phe(6)-Pro(7)-Leu(8)]), with all-trans peptide bond geometry, was elucidated by a combination of 2D NMR methods and tandem mass spectrometry. The solution state conformation was determined by ROE restrained molecular dynamics calculations. The structural features were found to be similar to those of the crystal structure of the cyclic decapeptide, phakellistatin 8, despite differing peptide sequences. (C) 2002 Elsevier Science Ltd. All rights reserved.

Original languageEnglish
Pages (from-to)7863-7868
Number of pages5
JournalTetrahedron
Volume58
DOIs
Publication statusPublished - 2002

Keywords

  • natural products
  • amino acids
  • peptides
  • Stylotella aurantium
  • sponge
  • nuclear magnetic resonance
  • mass spectrometry
  • restrained molecular dynamics
  • solution conformation
  • ASCIDIAN LISSOCLINUM-PATELLA
  • ANTINEOPLASTIC AGENTS
  • CONFORMATION
  • GROWTH
  • PHAKELLISTATIN-8
  • CYCLOPEPTIDES
  • ANTAMANIDE
  • CARTERI

Cite this

Axinellin C, a proline-rich cyclic octapeptide isolated from the Fijian marine sponge Stylotella aurantium. / Tabudravu, Jioji Natadra; Morris, L. A.; Kettenes-van den Bosch, J. J.; Jaspars, Marcel.

In: Tetrahedron, Vol. 58, 2002, p. 7863-7868.

Research output: Contribution to journalArticle

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abstract = "The structure of a new cyclic octapeptide, axinellin C, (cyclo[Thr(1)-Val(2)-Pro(3)-Trp(4)-Pro(5)-Phe(6)-Pro(7)-Leu(8)]), with all-trans peptide bond geometry, was elucidated by a combination of 2D NMR methods and tandem mass spectrometry. The solution state conformation was determined by ROE restrained molecular dynamics calculations. The structural features were found to be similar to those of the crystal structure of the cyclic decapeptide, phakellistatin 8, despite differing peptide sequences. (C) 2002 Elsevier Science Ltd. All rights reserved.",
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AU - Morris, L. A.

AU - Kettenes-van den Bosch, J. J.

AU - Jaspars, Marcel

PY - 2002

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AB - The structure of a new cyclic octapeptide, axinellin C, (cyclo[Thr(1)-Val(2)-Pro(3)-Trp(4)-Pro(5)-Phe(6)-Pro(7)-Leu(8)]), with all-trans peptide bond geometry, was elucidated by a combination of 2D NMR methods and tandem mass spectrometry. The solution state conformation was determined by ROE restrained molecular dynamics calculations. The structural features were found to be similar to those of the crystal structure of the cyclic decapeptide, phakellistatin 8, despite differing peptide sequences. (C) 2002 Elsevier Science Ltd. All rights reserved.

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KW - peptides

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KW - nuclear magnetic resonance

KW - mass spectrometry

KW - restrained molecular dynamics

KW - solution conformation

KW - ASCIDIAN LISSOCLINUM-PATELLA

KW - ANTINEOPLASTIC AGENTS

KW - CONFORMATION

KW - GROWTH

KW - PHAKELLISTATIN-8

KW - CYCLOPEPTIDES

KW - ANTAMANIDE

KW - CARTERI

U2 - 10.1016/S0040-4020(02)00898-0

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JF - Tetrahedron

SN - 0040-4020

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