Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa

Sabrin R M Ibrahim, Cho Cho Min, Franka Teuscher, Rainer Ebel, Christel Kakoschke, Wenhan Lin, Victor Wray, RuAngelie Edrada-Ebel, Peter Proksch

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

Bioassay guided fractionation of the EtOAc fraction of the sponge Callyspongia aerizusa yielded seven new cytotoxic cyclic peptides callyaerins A-F (1-6) and H (8). Their structures were determined using extensive 1D (1H, 13C and DEPT) and 2D (COSY, HMQC, HMBC, TOCSY, and ROESY) NMR and mass spectral (ESI and HRESI-TOF) data. All compounds were cyclic peptides containing ring systems of 5-9 amino acids and side chains of 2-5 amino acids in length. An unusual (Z)-2,3-diaminoacrylic acid unit provided the template for ring closure and afforded the linkage to the peptidic side chain which was always initiated with a proline moiety. All peptides contained three or more proline residues and the remaining residues were predominantly hydrophobic residues with all amino acids present in the l form. Callyaerins A-F (1-6) and H (8) showed biological activity in antibacterial assays and in various cytotoxicity assays employing different tumour cell-lines (L5178Y, HeLa, and PC12). Callyaerins E (5) and H (8) exhibited strong activity against the L5178Y cell line with ED50 values of 0.39 and 0.48 microM, respectively. On the other hand, callyaerin A (1) showed strong inhibitory properties towards C. albicans.
LanguageEnglish
Pages4947-56
Number of pages10
JournalBioorganic and Medicinal Chemistry
Volume18
Issue number14
DOIs
Publication statusPublished - 2010

Fingerprint

Callyspongia
Cyclic Peptides
Porifera
Amino Acids
Proline
Assays
Cells
Bioassay
Cytotoxicity
Fractionation
Bioactivity
Tumor Cell Line
Biological Assay
Tumors
Nuclear magnetic resonance
Cell Line
Peptides
Acids
callyaerin A

Keywords

  • animals
  • anti-infective agents
  • antineoplastic agents
  • bacteria
  • bacterial infections
  • callyspongia aerizusa
  • candida albicans
  • candidiasis
  • cell line
  • drug screening assays
  • molecular structure
  • neoplasms
  • peptides

Cite this

Ibrahim, S. R. M., Min, C. C., Teuscher, F., Ebel, R., Kakoschke, C., Lin, W., ... Proksch, P. (2010). Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa. Bioorganic and Medicinal Chemistry , 18(14), 4947-56. https://doi.org/10.1016/j.bmc.2010.06.012
Ibrahim, Sabrin R M ; Min, Cho Cho ; Teuscher, Franka ; Ebel, Rainer ; Kakoschke, Christel ; Lin, Wenhan ; Wray, Victor ; Edrada-Ebel, RuAngelie ; Proksch, Peter. / Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa. In: Bioorganic and Medicinal Chemistry . 2010 ; Vol. 18, No. 14. pp. 4947-56.
@article{ad16b352b5b84c378e495d6a7c1ee009,
title = "Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa",
abstract = "Bioassay guided fractionation of the EtOAc fraction of the sponge Callyspongia aerizusa yielded seven new cytotoxic cyclic peptides callyaerins A-F (1-6) and H (8). Their structures were determined using extensive 1D (1H, 13C and DEPT) and 2D (COSY, HMQC, HMBC, TOCSY, and ROESY) NMR and mass spectral (ESI and HRESI-TOF) data. All compounds were cyclic peptides containing ring systems of 5-9 amino acids and side chains of 2-5 amino acids in length. An unusual (Z)-2,3-diaminoacrylic acid unit provided the template for ring closure and afforded the linkage to the peptidic side chain which was always initiated with a proline moiety. All peptides contained three or more proline residues and the remaining residues were predominantly hydrophobic residues with all amino acids present in the l form. Callyaerins A-F (1-6) and H (8) showed biological activity in antibacterial assays and in various cytotoxicity assays employing different tumour cell-lines (L5178Y, HeLa, and PC12). Callyaerins E (5) and H (8) exhibited strong activity against the L5178Y cell line with ED50 values of 0.39 and 0.48 microM, respectively. On the other hand, callyaerin A (1) showed strong inhibitory properties towards C. albicans.",
keywords = "animals, anti-infective agents, antineoplastic agents, bacteria, bacterial infections, callyspongia aerizusa, candida albicans, candidiasis, cell line, drug screening assays, molecular structure, neoplasms, peptides",
author = "Ibrahim, {Sabrin R M} and Min, {Cho Cho} and Franka Teuscher and Rainer Ebel and Christel Kakoschke and Wenhan Lin and Victor Wray and RuAngelie Edrada-Ebel and Peter Proksch",
note = "Copyright (c) 2010 Elsevier Ltd. All rights reserved.",
year = "2010",
doi = "10.1016/j.bmc.2010.06.012",
language = "English",
volume = "18",
pages = "4947--56",
journal = "Bioorganic and Medicinal Chemistry",
issn = "0968-0896",
number = "14",

}

Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa. / Ibrahim, Sabrin R M; Min, Cho Cho; Teuscher, Franka; Ebel, Rainer; Kakoschke, Christel; Lin, Wenhan; Wray, Victor; Edrada-Ebel, RuAngelie; Proksch, Peter.

In: Bioorganic and Medicinal Chemistry , Vol. 18, No. 14, 2010, p. 4947-56.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa

AU - Ibrahim, Sabrin R M

AU - Min, Cho Cho

AU - Teuscher, Franka

AU - Ebel, Rainer

AU - Kakoschke, Christel

AU - Lin, Wenhan

AU - Wray, Victor

AU - Edrada-Ebel, RuAngelie

AU - Proksch, Peter

N1 - Copyright (c) 2010 Elsevier Ltd. All rights reserved.

PY - 2010

Y1 - 2010

N2 - Bioassay guided fractionation of the EtOAc fraction of the sponge Callyspongia aerizusa yielded seven new cytotoxic cyclic peptides callyaerins A-F (1-6) and H (8). Their structures were determined using extensive 1D (1H, 13C and DEPT) and 2D (COSY, HMQC, HMBC, TOCSY, and ROESY) NMR and mass spectral (ESI and HRESI-TOF) data. All compounds were cyclic peptides containing ring systems of 5-9 amino acids and side chains of 2-5 amino acids in length. An unusual (Z)-2,3-diaminoacrylic acid unit provided the template for ring closure and afforded the linkage to the peptidic side chain which was always initiated with a proline moiety. All peptides contained three or more proline residues and the remaining residues were predominantly hydrophobic residues with all amino acids present in the l form. Callyaerins A-F (1-6) and H (8) showed biological activity in antibacterial assays and in various cytotoxicity assays employing different tumour cell-lines (L5178Y, HeLa, and PC12). Callyaerins E (5) and H (8) exhibited strong activity against the L5178Y cell line with ED50 values of 0.39 and 0.48 microM, respectively. On the other hand, callyaerin A (1) showed strong inhibitory properties towards C. albicans.

AB - Bioassay guided fractionation of the EtOAc fraction of the sponge Callyspongia aerizusa yielded seven new cytotoxic cyclic peptides callyaerins A-F (1-6) and H (8). Their structures were determined using extensive 1D (1H, 13C and DEPT) and 2D (COSY, HMQC, HMBC, TOCSY, and ROESY) NMR and mass spectral (ESI and HRESI-TOF) data. All compounds were cyclic peptides containing ring systems of 5-9 amino acids and side chains of 2-5 amino acids in length. An unusual (Z)-2,3-diaminoacrylic acid unit provided the template for ring closure and afforded the linkage to the peptidic side chain which was always initiated with a proline moiety. All peptides contained three or more proline residues and the remaining residues were predominantly hydrophobic residues with all amino acids present in the l form. Callyaerins A-F (1-6) and H (8) showed biological activity in antibacterial assays and in various cytotoxicity assays employing different tumour cell-lines (L5178Y, HeLa, and PC12). Callyaerins E (5) and H (8) exhibited strong activity against the L5178Y cell line with ED50 values of 0.39 and 0.48 microM, respectively. On the other hand, callyaerin A (1) showed strong inhibitory properties towards C. albicans.

KW - animals

KW - anti-infective agents

KW - antineoplastic agents

KW - bacteria

KW - bacterial infections

KW - callyspongia aerizusa

KW - candida albicans

KW - candidiasis

KW - cell line

KW - drug screening assays

KW - molecular structure

KW - neoplasms

KW - peptides

UR - http://www.scopus.com/inward/record.url?scp=77955325025&partnerID=8YFLogxK

U2 - 10.1016/j.bmc.2010.06.012

DO - 10.1016/j.bmc.2010.06.012

M3 - Article

VL - 18

SP - 4947

EP - 4956

JO - Bioorganic and Medicinal Chemistry

T2 - Bioorganic and Medicinal Chemistry

JF - Bioorganic and Medicinal Chemistry

SN - 0968-0896

IS - 14

ER -