Purification and primary structure of two isoforms of arenicin, a novel antimicrobial peptide from marine polychaeta <i>Arenicola marina</i>

Ovchinnikova, Tatiana V.; Алешина, Г. М.; Balandin, Sergey V.; Krasnosdembskaya, Anna D.; Markelov, Mikhail L.; Frolova, Elena I.; Leonova, Yulia F.; Tagaev, Andrey A.; Krasnodembsky, Eugeny G.; Kokryakov, V. N.

doi:10.1016/j.febslet.2004.10.012

Cited by 138 publications

(135 citation statements)

References 40 publications

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“…[8][9][10] Earlier we discovered two novel 21-residue AMPs, termed arenicins, from coelomocytes of marine polychaeta lugworm Arenicola marina. 11 Both arenicin-1 (RWCVYAYVRVRGVLV-RYRRCW, 2758.3 Da) and arenicin-2 (RWCVYAYVRIRGVLV-RYRRCW, 2772.3 Da) exhibit potent activity against Grampositive and Gram-negative bacteria and fungi. Each isoform has one disulfide bond (Cys3-Cys20) forming a 18-residue ring.…”

Section: Introductionmentioning

confidence: 99%

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Molecular insight into mechanism of antimicrobial action of the β‐hairpin peptide arenicin: Specific oligomerization in detergent micelles

et al. 2007

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Arenicins are 21‐residue cationic antimicrobial peptides isolated from marine polychaeta Arenicola marina. The peptides exhibit potent broad‐spectrum antimicrobial activity. In water solution arenicin‐2 adopts a β‐hairpin conformation, stabilized by one disulfide and nine hydrogen bonds. To determine the propensity for the peptide oligomerization in membrane mimetic systems, the recombinant arenicin‐2 was overexpressed as a fused form in Escherichia coli. The arenicin‐2 oligomerization and intermolecular packing in membrane mimicking environment were investigated using high‐resolution NMR spectroscopy. The present studies show that arenicin‐2 preserves a β‐hairpin structure and forms asymmetric dimers upon incorporation into the dodecylphosphocholine micelle. Two monomers of arenicin‐2 are aligned parallel to each other by the N‐terminal strands of the β‐hairpin (CN↑↑NC type of association). Polyacrylamide gel electrophoresis analysis indicated that in environment of anionic SDS micelles the arenicin‐2 might undergo further oligomerization and form tetramers. Our results afford further molecular insight into possible mechanism of antimicrobial action of arenicins. © 2007 Wiley Periodicals, Inc. Biopolymers 89: 455–464, 2008.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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Section: Introductionmentioning

confidence: 99%

“…12 Arenicin has efficient and broad-spectrum antimicrobial activity. 11 Yet, molecular mechanism of the peptide selective interaction with the cell membranes of the target microorganisms is obscure. Molecular details of the peptide-lipid interactions, disruption, and/or translocation across target membranes generate considerable interest.…”

Section: Introductionmentioning

confidence: 99%

Molecular insight into mechanism of antimicrobial action of the β‐hairpin peptide arenicin: Specific oligomerization in detergent micelles

et al. 2007

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“…. peptide (Matsunaga et al, 1985), (Ovchinnikova et al, 2004), (Iijima et al, 2003), (Charlet et al, 1996;Mitta et al, 1999;Mitta et al, 2000), (Miyata et al, 1989;Saito et al, 1995), (Destoumieux et al, 1997) .…”

Section: 서 론mentioning

confidence: 99%

Isolation and Purification of an Antimicrobial Material from the Jellyfish Nemopilema nomurai

문호성¹,

김연계²,

이문희³

et al. 2011

Korean Journal of Fisheries and Aquatic Sciences

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An antimicrobial material was purified from the acidified whole body extract of the jellyfish Nemopilema nomurai by using C18 reversed phase and cation-exchange high performance liquid chromatography (HPLC). Whole body extract and the purified compound (JAP-1) showed potent antimicrobial activities against a wide range of microorganisms including Escherichia coli D31, Bacillus subtilis, Streptococcus iniae and Candida albicans, without significant hemolytic activity. Treatment of JAP-1 with trypsin completely abolished all antibacterial activity against Bacillus subtilis, suggesting that JAP-1 is likely to be a proteinaceous antibiotic. The molecular weight of JAP-1 was determined to be 680.10 Da by MALDI-TOF mass spectroscopy.

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“…The bioactive compound has been isolated from a marine annelid, Arenicola marina by Mynderse et al, (1997). The compound arenicins are 21 residue peptides, which were completely killed E. coli within 5 mins at a concentration of 5μM probably by membrane permeablization (Ovchinnikova et al, 2004). Another peptide named perinerin from annelid has been purified from the clamworm Perinereis aibuhitensis (Pan et al, 2004).…”

Section: Bioactive Compounds From Annelidamentioning

confidence: 99%

Bioactive Compounds from Marine Invertebrates for Potential Medicines - An Overview

Datta¹,

Talapatra

Swarnakar

2015

ILNS

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The present review deals with the bioactive compounds of the marine non-chordates. The potent medicinal usage of the bioactive compounds viz. steroids, terpenoids, isoprenoid and non-isoprenoid compounds, quinones, brominated compounds, nitrogen heterocyclics and nitrogen-sulphur heterocyclics from marine non-chordates have been compiled. Various literatures survey revealed that the bioactive compounds isolated in recent past from the marine poriferans, cnidarians, annelids, arthropods, molluscs and echinoderms could be rich sources of therapeutic agents having antibacterial, antiinflamatory, anticarcinogenic properties. In overall, the present study will be benefitted to know global drug discovery researches on bioactive compounds from marine organisms for students, scholars, scientists, pharmaceutical sector, and government regulating authorities as new challenging technology in clinical applications through medicines.

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Purification and primary structure of two isoforms of arenicin, a novel antimicrobial peptide from marine polychaeta Arenicola marina

Cited by 138 publications

References 40 publications

Molecular insight into mechanism of antimicrobial action of the β‐hairpin peptide arenicin: Specific oligomerization in detergent micelles

Molecular insight into mechanism of antimicrobial action of the β‐hairpin peptide arenicin: Specific oligomerization in detergent micelles

Isolation and Purification of an Antimicrobial Material from the Jellyfish Nemopilema nomurai

Bioactive Compounds from Marine Invertebrates for Potential Medicines - An Overview

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