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

doi:10.1016/j.bmc.2010.06.012

Cited by 82 publications

(109 citation statements)

References 35 publications

Supporting

Mentioning

104

Contrasting

Unclassified

Order By: Relevance

“…The ESIMS spectrum gave a basic fragment ion peak at m/z 861 for [M − (Pro+2Ile+Asn+Ala+NH 2 )] + , further supporting the composition of the side chain as previously reported. 5 In the same manner, ROESY correlations between the amide protons of the cyclic moiety disclosed the presence of the partial peptide sequences Leu R7 -DAA-Ile R1 and Ile R3 -Phe R4 . The connectivity of these two fragments was justified based on ROESY cross-peaks between Ile R3 -NH/Hyp R2 -Hα, Phe R4 -NH/ 3 0.71, d (6.6) C2-β, C2-γ, C2-δ C3 Phe NH 7.64,d (9.2) C3-α, C3-β, C2-CO C2-α, C4-NH, C2-NH CO 170.9, C α 54.…”

Section: Articlementioning

confidence: 94%

“…8,12 The remaining residues are predominantly hydrophobic amino acids such as IIe, Leu, Val, and Phe, with all amino acids present in the L-configuration. Apart from our previous reports on this class of peptides, 5,6 there is only one further example, callynormine A, which had been isolated from the Kenyan sponge Callyspongia abnormis. 7 Thus, this intriguing class of peptides is currently restricted to the sponge genus Callyspongia.…”

Section: Journal Of Natural Productsmentioning

confidence: 95%

“…5 It was speculated that DAA biogenetically arises from oxidation of a serine or cysteine unit to give a formyl glycine, which will undergo Schiff base formation with the amino group of the next amino acid in the ring, followed by double-bond migration. 7 This endiamino group is of special interest, as it is expected to introduce rigidity into cyclic peptide structures.…”

Section: Journal Of Natural Productsmentioning

confidence: 99%

See 2 more Smart Citations

Callyaerins from the Marine Sponge Callyspongia aerizusa: Cyclic Peptides with Antitubercular Activity

Kalscheuer¹,

Koliwer‐Brandl²,

Hartmann

et al. 2015

J. Nat. Prod.

Self Cite

View full text Add to dashboard Cite

Chemical investigation of the Indonesian sponge Callyspongia aerizusa afforded five new cyclic peptides, callyaerins I-M (1-5), along with the known callyaerins A-G (6-12). The structures of the new compounds were unambiguously elucidated on the basis of one- and two-dimensional NMR spectroscopy and mass spectrometry. In addition, the structures of callyaerins D (9), F (11), and G (12), previously available in only small amounts, have been reinvestigated and revised. All compounds were tested in vitro against Mycobacterium tuberculosis, as well as against THP-1 (human acute monocytic leukemia) and MRC-5 (human fetal lung fibroblast) cell lines, in order to assess their general cytotoxicity. Callyaerins A (6) and B (7) showed potent anti-TB activity with MIC₉₀ values of 2 and 5 μM, respectively. Callyaerin C (8) was found to be less active, with an MIC₉₀ value of 40 μM. Callyaerin A (6), which showed the strongest anti-TB activity, was not cytotoxic to THP-1 or MRC-5 cells (IC₅₀ > 10 μM), which highlights the potential of these compounds as promising anti-TB agents.

show abstract

Section: Articlementioning

confidence: 94%

Section: Journal Of Natural Productsmentioning

confidence: 95%

Section: Journal Of Natural Productsmentioning

confidence: 99%

See 1 more Smart Citation

Callyaerins from the Marine Sponge Callyspongia aerizusa: Cyclic Peptides with Antitubercular Activity

Kalscheuer¹,

Koliwer‐Brandl²,

Hartmann

et al. 2015

J. Nat. Prod.

Self Cite

View full text Add to dashboard Cite

show abstract

“…2). In the NOESY spectrum diagnostic NOE correlations were observed between a-H and NH of adjacent residues unambiguously identified the following amide linkage: H-8/2-NH (d H 4.56/9.10), (Ibrahim et al, 2010(Ibrahim et al, , 2008Marfey 1984) followed by HPLC analysis with co-injection of standard amino acids. The amino acids were identified to be L-Asn L-Leu and L-Ile.…”

Section: Resultsmentioning

confidence: 95%

Staphylopeptide A, a new cyclic tetrapeptide from culture broth of Staphylococcus sp.

Khedr

Mohamed

Orabi

et al. 2015

Phytochemistry Letters

Self Cite

View full text Add to dashboard Cite

“…Standards of l and d amino acids were treated separately with FDNPL in the same manner. The FDNPL derivatives were analyzed using LC-MS by comparison of the retention time and molecular weight with those of standard amino acids FDNPL derivatives [22,23]. …”

Section: Methodsmentioning

confidence: 99%

Theonellamide G, a Potent Antifungal and Cytotoxic Bicyclic Glycopeptide from the Red Sea Marine Sponge Theonella swinhoei

et al. 2014

View full text Add to dashboard Cite

In our search for bioactive metabolites from marine organisms, we have investigated the polar fraction of the organic extract of the Red Sea sponge Theonella swinhoei. Successive chromatographic separations and final HPLC purification of the potent antifungal fraction afforded a new bicyclic glycopeptide, theonellamide G (1). The structure of the peptide was determined using extensive 1D and 2D NMR and high-resolution mass spectral determinations. The absolute configuration of theonellamide G was determined by chemical degradation and 2D NMR spectroscopy. Theonellamide G showed potent antifungal activity towards wild and amphotericin B-resistant strains of Candida albicans with IC50 of 4.49 and 2.0 μM, respectively. Additionally, it displayed cytotoxic activity against the human colon adenocarcinoma cell line (HCT-16) with IC50 of 6.0 μM. These findings provide further insight into the chemical diversity and biological activities of this class of compounds.

show abstract

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

Cited by 82 publications

References 35 publications

Callyaerins from the Marine Sponge Callyspongia aerizusa: Cyclic Peptides with Antitubercular Activity

Callyaerins from the Marine Sponge Callyspongia aerizusa: Cyclic Peptides with Antitubercular Activity

Staphylopeptide A, a new cyclic tetrapeptide from culture broth of Staphylococcus sp.

Theonellamide G, a Potent Antifungal and Cytotoxic Bicyclic Glycopeptide from the Red Sea Marine Sponge Theonella swinhoei

Contact Info

Product

Resources

About