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At least 127 records · Page 7Linked to original sources
PubMed1998

A depsipeptide fungal metabolite inhibitor of cholesteryl ester transfer protein.

The organic extract of the fermentation broth of a fungus was found to contain a depsipeptide SCH 58149 (1), containing three amino acids and a beta-hydroxy acid, by spectroscopic studies. The amino acids were phenyl alanine, alanine and leucine and the beta-hydroxy acid is 3-hydroxy-4-methyl octanoic acid. SCH 58149 exhibited weak activity against cholesterol ester transfer protein (CETP) with an IC50 of 50 microM.

Acremonium↗
PubMed2004

Localization of the antimitotic peptide and depsipeptide binding site on beta-tubulin.

Several naturally occurring peptides and depsipeptides which include the cryptophycins, dolastatin 10, hemiasterlin, and phomopsin A have been found to be potent antimitotic agents, causing cell death at picomolar or low nanomolar concentrations. These compounds inhibit microtubule growth, modulate the dynamics of microtubules, and induce the self-association of tubulin dimers into single-walled rings and spirals. These peptides exhibit mutual competitive inhibition in binding to beta-tubulin, while noncompetitively inhibiting the binding of vinblastine and vincristine to beta-tubulin. Despite the abundance of biochemical information, the details of their molecular interactions with tubulin are not known. In this study, using a combination of molecular dynamics simulations and molecular docking studies, a common binding site for cryptophycin 1, cryptophycin 52, dolastatin 10, hemiasterlin, and phomopsin A on beta-tubulin has been identified. Application of these same methods to alpha-tubulin indicated no interaction between alpha-tubulin and any of the peptides. On the basis of the docking results, a model for the mechanism of microtubule disruption and formation of aberrant nonmicrotubule structures is proposed. Both the active site and mechanism of microtubule depolymerization predictions are in good agreement with experimental findings.

Amino Acid Sequence↗
PubMed2001

Halipeptins A and B: two novel potent anti-inflammatory cyclic depsipeptides from the Vanuatu marine sponge Haliclona species.

Two new metabolites, named halipeptins A and B, have been isolated from the marine sponge Haliclona sp. Their structures were determined by extensive use of one- and two-dimensional NMR experiments, mass spectrometry, and UV and IR spectroscopy. Halipeptin A is a novel 17-membered cyclic depsipeptide, consisting of five residues including two alanines (with L stereochemistry) and three new residues that appear to be previously undescribed from natural sources: 1,2-oxazetidine-4-methyl-4-carboxylic acid, 3-hydroxy-2,2,4-trimethyl-7-methoxydecanoic acid (HTMMD), and N-methyl-delta-hydroxyisoleucine. The HTMMD residue is substituted with 3-hydroxy-2,2,4-trimethyl-7-hydroxydecanoic acid in halipeptin B. Halipeptin A was found to possess very potent anti-inflammatory activity in vivo, causing about 60% inhibition of edema in mice at the dose of 300 microg/kg (i.p.).

Animals↗
PubMed2002

Kulokekahilide-1, a cytotoxic depsipeptide from the cephalaspidean mollusk Philinopsis speciosa.

The cytotoxic depsipeptide kulokekahilide-1, which contains two unusual amino acids, 4-phenylvaline and 3-amino-2-methylhexanoic acid, was isolated from the cephalaspidean mollusk Philinopsis speciosa. Structure elucidation of kulokekahilide-1 was carried out by spectroscopic analysis and chemical degradation. The absolute stereochemistry was determined by Marfey analysis for amino acids and chiral HPLC analysis for hydroxy acids. All four stereoisomers of 4-phenylvaline and 3-amino-2-methylhexanoic acid, which were necessary for Marfey analysis, were synthesized by use of the Heck reaction and Evans's method, respectively. Kulokekahilide-1 showed cytotoxicity against P388 murine leukemia cells with an IC(50) value of 2.1 microg/mL.

Amino Acid Sequence↗
PubMed2003

Total synthesis of the depsipeptide FR-901375.

The first total synthesis of FR-901375, a novel bicyclic depsipeptide isolated from the fermentation broth of Pseudomonas chloroaphis No. 2522, has been achieved. The synthetic approach involves 13 reaction steps and is achieved in 12% overall yield. The key points in the successful synthetic strategy are a concise asymmetric synthesis of the key building block (3R,4E)-3-hydroxy-7-mercapto-4-heptenoic acid, a mild Mitsunobu macrolactonization step, and an I(2)-mediated deprotection with concomitant disulfide-bridge formation.

Depsipeptides↗
PubMed2000

Tamandarins A and B: new cytotoxic depsipeptides from a Brazilian ascidian of the family Didemnidae.

The structures of two new, naturally occurring cytotoxic depsipeptides, tamandarins A and B (1 and 2), are presented. The tamandarins were isolated from an unidentified Brazilian marine ascidian of the family Didemnidae. The structures of the new cytotoxins were assigned by interpretation of FABMS data and by extensive 2D NMR analyses. The absolute configurations of the tamandarins were assigned by acid and alkaline hydrolysis to yield their corresponding amino acids, which were then analyzed as their Marfey derivatives. The cytotoxicity of tamandarin A (1) was evaluated against various human cancer cell lines and shown to be slightly more potent than didemnin B. A qualitative discussion of the conformation of tamandarin A (1) in solution, obtained from NMR J-value data, variable temperature experiments, and NOESY/ROESY data, is included.

Animals↗
PubMed2001

Microspinosamide, a new HIV-inhibitory cyclic depsipeptide from the marine sponge Sidonops microspinosa.

Microspinosamide (1), a new cyclic depsipeptide incorporating 13 amino acid residues, was isolated from extracts of an Indonesian collection of the marine sponge Sidonops microspinosa. Its structure was elucidated by extensive NMR and mass spectral analyses, and by chemical degradation and derivatization studies. The tridecapeptide 1 incorporates numerous uncommon amino acids, and it is the first naturally occurring peptide to contain a beta-hydroxy-p-bromophenylalanine residue. Microspinosamide (1) inhibited the cytopathic effect of HIV-1 infection in an XTT-based in vitro assay with an EC(50) value of approximately 0.2 microg/mL.

Animals↗
PubMed2001

Georgamide, a new cyclic depsipeptide with an alkynoic acid residue from an Australian cyanobacterium.

A cyclic depsipeptide, georgamide (1), was isolated from an Australian cyanobacterium and characterized by spectroscopic means. The constituent units were five amino acid residues, one each of L-Thr, L-Pro, L-Val, N-Me-L-Val, and N-Me-L-Phe, and two hydroxy carboxylic acids, 2(S)-hydroxy-3(R)-methylpentanoic acid and the unusual 2,2-dimethyl-3-hydroxy-7-octynoic acid. The stereochemistry was determined by hydrolysis of the peptide followed by derivatization and HPLC comparison with standard samples.

Amino Acids↗
PubMed2001

Somamides A and B, two new depsipeptide analogues of dolastatin 13 from a Fijian cyanobacterial assemblage of Lyngbya majuscula and Schizothrix species.

Somamides A (1) and B (2) were isolated from assemblages of the marine cyanobacteria Lyngbya majusculaand Schizothrix sp. from the Fijian Islands. These new depsipeptides are analogous in structure to the cyanobacterial metabolite symplostatin 2 (4) as well as dolastatin 13 (3), originally isolated from Dolabella auricularia, further demonstrating the cyanobacterial origin of the dolastatins.

Amino Acids↗
PubMed2002

Isolation and structure determination of obyanamide, a novel cytotoxic cyclic depsipeptide from the marine cyanobacterium Lyngbya confervoides.

Obyanamide (1) was isolated from a variety of the marine cyanobacterium Lyngbya confervoides collected in Saipan, Commonwealth of the Northern Mariana Islands. Gross structure elucidation of this novel cyclic depsipeptide relied on extensive application of 2D NMR techniques. The absolute stereochemistry was deduced by chiral chromatography of the hydrolysis products and comparison with authentic and synthetic standards. Obyanamide (1) was cytotoxic against KB cells with an IC(50) of 0.58 microg/mL.

Antineoplastic Agents↗
PubMed2003

Tasipeptins A and B: new cytotoxic depsipeptides from the marine cyanobacterium Symploca sp.

Two new depsipeptides have been isolated from a Symploca sp. collected in Palau. The gross structures of tasipeptins A (1) and B (2) were determined by standard spectroscopic techniques, and the absolute configuration of the amino acid units was determined by chiral HPLC. The relative stereochemistry of the 3-amino-6-hydroxy-2-piperidone (Ahp) moiety in both structures was determined by analysis of (2,3)J(H,H) values. Oxidation with PCC and acid hydrolysis unmasked this latent glutamic acid moiety, allowing for elucidation of the total configuration of 1 and 2. Tasipeptins A (1) and B (2) were cytotoxic toward KB cells with IC(50) values of 0.93 and 0.82 microM, respectively.

Antineoplastic Agents↗
PubMed2003

Ulongapeptin, a cytotoxic cyclic depsipeptide from a Palauan marine cyanobacterium Lyngbya sp.

Ulongapeptin (1), a cyclic depsipeptide, was isolated from a Palauan marine cyanobacterium Lyngbya sp. The gross structure was elucidated through one-dimensional TOCSY experiments and other spectroscopic techniques. The absolute and relative stereochemistry of the beta-amino acid, 3-amino-2-methyl-7-octynoic acid (AMO), in 1 was determined by synthesis of the saturated alpha-alkyl-beta-amino acid and Marfey's analysis of the acid hydrolysate of tetrahydro-1. Ulongapeptin (1) was cytotoxic against KB cells at an IC(50) value of 0.63 microM.

Antineoplastic Agents↗
PubMed2004

Neamphamide A, a new HIV-inhibitory depsipeptide from the Papua New Guinea marine sponge Neamphius huxleyi.

A new HIV-inhibitory cyclic depsipeptide, neamphamide A (2), was isolated from a Papua New Guinea collection of the marine sponge Neamphius huxleyi. Its structure was established through interpretation of spectroscopic data and by acid hydrolysis, derivatization of the free amino acids, and LC-MS analysis of the derivatives. Neamphamide A (2) contains 11 amino acid residues and an amide-linked 3-hydroxy-2,4,6-trimethylheptanoic acid moiety. The amino acid constituents were identified as L-Leu, L-NMeGln, D-Arg, D- and L-Asn, two residues of D-allo-Thr, L-homoproline, (3S,4R)-3,4-dimethyl-L-glutamine, beta-methoxytyrosine, and 4-amino-7-guanidino-2,3-dihydroxyheptanoic acid. In a cell-based XTT assay, 2 exhibited potent cytoprotective activity against HIV-1 infection with an EC50 of approximately 28 nM.

Animals↗
PubMed2006

Kutznerides 1-4, depsipeptides from the actinomycete Kutzneria sp. 744 inhabiting mycorrhizal roots of Picea abies seedlings.

Bioassay-guided fractionation of culture supernatants of the actinomycete Kutzneria sp. 744 resulted in the isolation of four new depsipeptides (1-4). Structure analysis revealed the general structure: cyclo[2-(1-methylcyclopropyl)-D-glycine-(2S,3aR,8aS)-6,7-dichloro-3a-hydroxy-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid-3-hydroxy-D-glutamic acid-O-methyl-L-serine-L-piperazic acid-(S)-2-hydroxy-3,3-dimethylbutanoic acid]. The 3-hydroxy-d-glutamic acid was present as its threo-isomer in 1 and 2 and as its erythro-isomer in 3 and 4. The piperazic acid was modified to its (R)-4-chloro analogue in 2 and to its C-5/N unsaturated analogue in 4. Compounds 1-4 displayed moderate spore germination inhibiting activity against several common root-rotting fungi.

Actinobacteria↗
PubMed2006

A chemical study of cyclic depsipeptides produced by a sponge-derived fungus.

Two novel cyclic depsipeptides, guangomides A (1) and B (2), together with a new destruxin derivative (3) were isolated from the cytotoxic extract obtained from the saltwater culture of an unidentifiable sponge-derived fungus. The new structures were elucidated on the basis of analysis of extensive 1D and 2D NMR data sets, and the absolute configurations of 2S, 9S, 13S, 19S, 24R, 28R of 1 were determined on the basis of the combined X-ray and Marfey's method structure analysis. Identical absolute configurations were assumed for 2. The cytotoxicity of the extract was found to be due to brefeldin A, while 1 and 2 showed weak antibacterial activity against Staphylococcus epidermidis and Enterococcus durans.

Animals↗
PubMed2000

A new depsipeptide from the sacoglossan mollusk Elysia ornata and the green alga Bryopsis species.

A new cyclic depsipeptide, kahalalide O (1), was isolated from the sacoglossan Elysia ornata and its algal diet Bryopsis sp. The structure was elucidated primarily by NMR and MS spectral methods, and the stereochemistry of the amino acid residues was determined by chiral HPLC and Marfey analyses. Unlike the related metabolite kahalalide F, which is in development as a potential anticancer agent, kahalalide O (1) was inactive in arresting the growth of P-388, A549, HT29, and MEL28 cancer cell lines in vitro.

Animals↗
PubMed2000

Malevamides A-C, new depsipeptides from the marine cyanobacterium Symploca laete-viridis.

Three new depsipeptides, malevamides A-C (1-3), were isolated from the cyanobacterium Symploca laete-viridis collected off the south shore of Oahu, Hawaii. Compounds 1-3 were identified by spectral methods, and partial stereochemical assignments were made by chiral HPLC of the hydrolyzed compounds. At a concentration of 2 microg/mL, compounds 1-3 were inactive against P-388, A-549, and HT-29 cancer cells.

Antineoplastic Agents↗
PubMed2002

Nagahamide A, an antibacterial depsipeptide from the marine sponge Theonella swinhoei.

[structure: see text] An antibacterial depsipeptide, nagahamide A (1), has been isolated from the marine sponge Theonella swinhoei. Its structure was determined on the basis of spectral and chemical methods. Absolute configuration of amino acid residues was determined by Marfey's analysis, and relative stereochemistry of the polyketide moiety was assigned by comparison of NMR data with those of a model compound.

Animals↗