Cyclodepsipeptides from Marine Sponges: Natural Agents for Drug Research

Andavan, Gowri Shankar Bagavananthem; Lemmens‐Gruber, Rosa

doi:10.3390/md8030810

Cited by 122 publications

(64 citation statements)

References 107 publications

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“…Among these, depsipeptides and cyclodepsipeptides stand out for their broad spectrum of biological activities and structural diversity [1][2][3] . The presence of several unique residues and the complex structural features shown by these natural products make their structural elucidation challenging.…”

mentioning

confidence: 99%

The first total synthesis of the cyclodepsipeptide pipecolidepsin A

et al. 2013

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Pipecolidepsin A is a head-to-side-chain cyclodepsipeptide isolated from the marine sponge Homophymia lamellosa. This compound shows relevant cytotoxic activity in three human tumour cell lines and has unique structural features, with an abundance of non-proteinogenic residues, including several intriguing amino acids. Although the moieties present in the structure show high synthetic difficulty, the cornerstone is constituted by the unprecedented and highly hindered g-branched b-hydroxy-a-amino acid D-allo-(2R,3R,4R)-2-amino-3-hydroxy-4,5-dimethylhexanoic acid (AHDMHA) residue, placed at the branching ester position and surrounded by the four demanding residues L-(2S,3S,4R)-3,4-dimethylglutamine, (2R,3R,4S)-4,7-diamino-2,3-dihydroxy-7-oxoheptanoic acid, D-allo-Thr and L-pipecolic acid. Here we describe the first total synthesis of a D-allo-AHDMHA-containing peptide, pipecolidepsin A, thus allowing chemical structure validation of the natural product and providing a robust synthetic strategy to access other members of the relevant head-to-side-chain family in a straightforward manner.

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confidence: 99%

The first total synthesis of the cyclodepsipeptide pipecolidepsin A

et al. 2013

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“…Neamphamide A, isolated from the marine sponge Neamphius huxleyi (Papua, New Guinea), is an HIV inhibitor [62]. The (2R)-diaminopropionic acid fragment with an unsubstituted β-amino group in the side chain of the linear pentapeptide is also present in the cyclic heptapeptide theopapuamide (32), isolated from the sponge Theonella swinhoei (Papua, New Guinea). Its ring also contains a lactone bond [60,63].…”

Section: Cyclic Peptides Papuamides -Hiv Inhibitorsmentioning

confidence: 99%

“…This metabolite contains a β-amino acid which is unsubstituted at the α-position and has 4-hydroxyphenyl substituent at the β-position; the β-amino acid is (R)-β-tyrosine, the carboxyl group of which forms not a peptide bond but an ester (lactone) bond in the ring. Jasplakinolide (or jaspamide) (13) Jaspamide possesses cytotoxic activity and, by exhibiting in vitro activity against 36 cell cultures of various tumors, is a prospective anticancer preparation [30][31][32]. Jaspamide also exhibits anthelminthic, insecticidal, and antifungal properties [7].…”

Section: Cyclic Peptides With Fragments Of β 3 -Arylamino Acidsmentioning

confidence: 99%

Biologically active cyclic polypeptides with fragments of β-amino acid derivatives isolated from marine organisms (review)

Romanova

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Rybalko

et al. 2011

Chem Heterocycl Comp

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Published data on the structure, stereochemistry, and biological activity of natural cyclic polypeptides containing fragments of β-amino acids are reviewed, and an attempt is made to relate the structure to the biological activity.According to available estimates [1], there are more β-amino acids in the nature than the 22 proteinogenic α-amino acids that take part in ribosomal protein synthesis. The β-amino acids exist either as such or as fragments of the molecules of natural compounds with various degrees of complexity [2] and most often as linear or cyclic peptides that are, in all probability, formed by such microorganisms as bacteria and fungi as a result of non-ribosomal protein synthesis [3].Before 1996 nothing was known about the structure of the simplest β-peptides in the crystal and in solution. Today there are numerous papers and reviews on natural, semisynthetic, and fully synthetic β-peptides, the most comprehensive of which are the papers [4][5][6]. For this reason we will not dwell on these aspects here.The aim of our review is to classify published data on the structure, stereochemistry, and biological activity and also to study the structure-activity relationship of cyclic β-peptides, which have shown greater resistance to the action of enzymes than their linear analogs and α-peptides and therefore exhibit biological selectivity.

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“…The broad bioactivity spectrum of marine peptides has high medicinal potential which attracts the attention of the pharmaceutical industry. Since the discovery of the first marine-derived antitumorcyclic peptide, ulithiacyclamide, many marine anticancerpeptides have entered into clinical trials with good prospects for drug development [4,5,6], such as kahalalide F, hemiasterlin, dolastatins, cemadotin, soblidotin, didemnins, aplidine, etc. [7].…”

Section: Introductionmentioning

confidence: 99%

Alkynyl-Containing Peptides of Marine Origin: A Review

et al. 2016

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Since the 1990s, a number of terminal alkynyl residue-containing cyclic/acyclic peptides have been identified from marine organisms, especially cyanobacteria and marine mollusks. This review has presented 66 peptides, which covers over 90% marine peptides with terminal alkynyl fatty acyl units. In fact, more than 90% of these peptides described in the literature are of cyanobacterial origin. Interestingly, all the linear peptides featured with terminal alkyne were solely discovered from marine cyanobacteria. The objective of this article is to provide an overview on the types, structural characterization of these unusual terminal alkynyl fatty acyl units, as well as the sources and biological functions of their composed peptides. Many of these peptides have a variety of biological activities, including antitumor, antibacterial, antimalarial, etc. Further, we have also discussed the evident biosynthetic origin responsible for formation of terminal alkynes of natural PKS (polyketide synthase)/NRPS (nonribosome peptide synthetase) hybrids.

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Cyclodepsipeptides from Marine Sponges: Natural Agents for Drug Research

Cited by 122 publications

References 107 publications

The first total synthesis of the cyclodepsipeptide pipecolidepsin A

The first total synthesis of the cyclodepsipeptide pipecolidepsin A

Biologically active cyclic polypeptides with fragments of β-amino acid derivatives isolated from marine organisms (review)

Alkynyl-Containing Peptides of Marine Origin: A Review

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