Jaspamide, a modified peptide from a Jaspis sponge, with insecticidal and antifungal activity

Zabriskie, T. Mark; Klocke, James A.; Ireland, Chris M.; Marcus, Andrew H.; Molinski, Tadeusz F.; Faulkner, D. John; Xu, Chaochao; Clardy, Jon

doi:10.1021/ja00271a062

Cited by 293 publications

(184 citation statements)

References 1 publication

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“…Prepsammaplin A (155) and psammaplins B (156), C (157), and D (158) were isolated from the marine sponge Psammaplysilla purpurea by Jimenez and Crews (110). The isolation of prepsammaplin A (155), a cysteine dimer, indicated that cysteine might be the precursor of the central part of psammaplin A. Interestingly, the R functional groups of psammaplin B (156) and C (157) are unique and do not appear to have counterparts among any known marine sponge amino acid derivatives (110).…”

Section: Oxime-histamines-ianthellinmentioning

confidence: 99%

The Marine Bromotyrosine Derivatives

Peng¹,

Jing²,

Hamann³

2005

The Alkaloids: Chemistry and Biology

101

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Section: Oxime-histamines-ianthellinmentioning

confidence: 99%

The Marine Bromotyrosine Derivatives

Peng¹,

Jing²,

Hamann³

2005

The Alkaloids: Chemistry and Biology

101

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“…Latrunculin B (37) is a macrolide toxin isolated from the Red Sea sponge Latrunculia magnifica (24). Jaspamide (38), a highly modified cyclic depsipeptide, was first identified from a sponge of the genus Jaspis (25).…”

Section: Marine-derived Compoundsmentioning

confidence: 99%

Marine Natural Products as Prototype Agrochemical Agents

Peng

Shen²,

Ka³

et al. 2003

J. Agric. Food Chem.

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In the interest of identifying new leads that could serve as prototype agrochemical agents, 18 structurally diverse marine-derived compounds were examined for insecticidal, herbicidal, and fungicidal activities. Several new classes of compounds have been shown to be insecticidal, herbicidal, and fungicidal, which suggests that marine natural products represent an intriguing source for the discovery of new agrochemical agents.

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“…Jaspamide is a metabolite of mixed peptide polyketide biosynthetic origin which has been proposed as a cyclic depsipeptide made up of 3 amino acids and an octyl ketide group (47). Eusynstyelamide is an extremely polar molecule isolated after methanol extraction which has been proposed to be a highly modified peptide dimer where each monomer is made up of two modified amino acids and a guanidinyl-amide group (41).…”

Section: Identification Of Bromotryptophan In Conus Peptide Toxinsmentioning

confidence: 99%

A Novel Post-translational Modification Involving Bromination of Tryptophan

Craig

Jimenéz

Dykert

et al. 1997

Journal of Biological Chemistry

100

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We report a novel post-translational modification involving halogenation of tryptophan in peptides recovered from the venom of carnivorous marine cone snails (Conus). The residue, L-6-bromotryptophan, was identified in the sequence of a heptapeptide, isolated from Conus imperialis, a worm-hunting cone. This peptide does not elicit gross behavioral symptoms when injected centrally or peripherally in mice. L-6-Bromotryptophan was also identified in a 33-amino acid peptide from Conus radiatus; this peptide has been shown to induce a sleep-like state in mice of all ages and is referred to as bromosleeper peptide. The sequences of the two peptides Pca-Cys-Gly-Gln-Ala-Trp*-Cys-NH 2 were determined using a combination of mass spectrometry, amino acid, and chemical sequence analyses, where Pca ‫؍‬ pyroglutamic acid, Hyp ‫؍‬ hydroxyproline, Gla ‫؍‬ ␥-carboxyglutamate, and Trp* ‫؍‬ L-6-bromotryptophan. The precise structure and stereochemistry of the modified residue were determined as L-6-bromotryptophan by synthesis, co-elution, and enzymatic hydrolysis experiments. To our knowledge this is the first documentation of tryptophan residues in peptides/proteins being modified in a eukaryotic system and the first report of halogenation of tryptophan in vivo. SEQUENCE 1 andPolypeptides encoded by genes are primarily made up of the 20 common amino acids that are directly translated using the genetic code. However, many of these amino acids can be further modified post-translationally to yield a set of additional amino acids that contribute to the function of the mature protein. Together the 20 primary amino acids and these "secondary" amino acids which are found in proteins comprise the set of proteinogenous amino acids.These modified amino acids include amino acid conjugates where the side chain is linked to a glycosyl, phosphate, or sulfate group and amino acids such as 5-hydroxylysine, 4-hydroxyproline, and ␥-carboxyglutamate. One notable set of modified amino acids are halogenated derivatives of tyrosine and histidine. Naturally occurring halogenated tyrosine and histidine residues have previously been identified from proteins (1-4). A particularly well documented example of in vivo posttranslational halogenation of an amino acid residue in a protein is afforded by thyroglobulin (5). After iodination of several tyrosine residues, selective cleavages release the iodinated thyroid hormones thyroxine (3,5,3Ј,5Ј-tetraiodothyronine or T 4 ) 1 ; 3,5,3Ј-triiodothyronine (T 3 ), and 3,3Ј-di-iodothyronine. The presence of free T 3 and T 4 has also been shown in protochordates, suggesting a primitive thyroid function exists in tunicates (2).Of the 20 common amino acids, alanine, glycine, isoleucine, leucine, and valine, which lack side chain functional groups, have not been implicated in post-translational modifications (6). In 1907 it was proposed that hydroxytryptophan was a proteinogenous amino acid (7), but this proposal has not been verified (1), and chemical oxidation of tryptophan is likely to be responsible for the observed ...

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Jaspamide, a modified peptide from a Jaspis sponge, with insecticidal and antifungal activity

Cited by 293 publications

References 1 publication

The Marine Bromotyrosine Derivatives

The Marine Bromotyrosine Derivatives

Marine Natural Products as Prototype Agrochemical Agents

A Novel Post-translational Modification Involving Bromination of Tryptophan

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