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

S.R.M. Ibrahim, C.C. Min, F. Teuscher, R. Ebel, C. Kakoschke, W. Lin, V. Wray, R. Edrada-Ebel, P. Proksch

Research output: Contribution to journalArticle

51 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 ( H, C 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 ED values of 0.39 and 0.48 µM, respectively. On the other hand, callyaerin A (1) showed strong inhibitory properties towards C. albicans.
Original languageEnglish
Pages (from-to)4947-4956
Number of pages10
JournalBioorganic & Medicinal Chemistry
Volume18
Issue number14
Early online date11 Jun 2010
DOIs
Publication statusPublished - 15 Jul 2010

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Cyclic Peptides
Amino Acids
Proline
Assays
Cells
Bioassay
Cytotoxicity
Fractionation
Bioactivity
Tumors
Nuclear magnetic resonance
Peptides
Acids
callyaerin A

Keywords

  • Callyspongia aerizusa
  • Callyaerins
  • Proline-rich cyclic peptides
  • Cytotoxicity
  • Antibacterial
  • Antifungal

Cite this

Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa. / Ibrahim, S.R.M.; Min, C.C.; Teuscher, F.; Ebel, R.; Kakoschke, C.; Lin, W.; Wray, V.; Edrada-Ebel, R.; Proksch, P.

In: Bioorganic & Medicinal Chemistry, Vol. 18, No. 14, 15.07.2010, p. 4947-4956.

Research output: Contribution to journalArticle

Ibrahim, SRM, Min, CC, Teuscher, F, Ebel, R, Kakoschke, C, Lin, W, Wray, V, Edrada-Ebel, R & Proksch, P 2010, 'Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa', Bioorganic & Medicinal Chemistry, vol. 18, no. 14, pp. 4947-4956. https://doi.org/10.1016/j.bmc.2010.06.012
Ibrahim, S.R.M. ; Min, C.C. ; Teuscher, F. ; Ebel, R. ; Kakoschke, C. ; Lin, W. ; Wray, V. ; Edrada-Ebel, R. ; Proksch, P. / Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa. In: Bioorganic & Medicinal Chemistry. 2010 ; Vol. 18, No. 14. pp. 4947-4956.
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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 ( H, C 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 ED values of 0.39 and 0.48 µM, respectively. On the other hand, callyaerin A (1) showed strong inhibitory properties towards C. albicans.",
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T1 - Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa

AU - Ibrahim, S.R.M.

AU - Min, C.C.

AU - Teuscher, F.

AU - Ebel, R.

AU - Kakoschke, C.

AU - Lin, W.

AU - Wray, V.

AU - Edrada-Ebel, R.

AU - Proksch, P.

N1 - S. R. M. Ibrahim wishes to thank the Egyptian Government for a scholarship. We are indebted to Professor Dr. W. E. G. Müller (Institute für Physiologische Chemie, Duesbergweg 6, D-55099 Mainz, Germany) for cytotoxicity testing. This project was supported by grants of the BMBF and MOST awarded to Professor Peter Proksch and Professor Wenhan Lin.

PY - 2010/7/15

Y1 - 2010/7/15

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 ( H, C 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 ED values of 0.39 and 0.48 µM, 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 ( H, C 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 ED values of 0.39 and 0.48 µM, respectively. On the other hand, callyaerin A (1) showed strong inhibitory properties towards C. albicans.

KW - Callyspongia aerizusa

KW - Callyaerins

KW - Proline-rich cyclic peptides

KW - Cytotoxicity

KW - Antibacterial

KW - Antifungal

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