FEBS Lett, 2004, 577(12):209-214

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

Two novel 21-residue antimicrobial peptides, arenicin-1 and arenicin-2, exhibiting activity against Gram-positive and Gram-negative bacteria and fungi, were purified from coelomocytes of marine polychaeta Arenicola marina (lugworm) by preparative gel electrophoresis and RP-HPLC. Molecular masses (2758.3 and 2772.3 Da) and complete amino acid sequences (RWCVYAYVRVRGVLVRYRRCW and RWCVYAYVRIRGVLVRYRRCW)The protein sequence data reported in this paper will appear in the Swiss-Prot and TrEMBL knowledgebase under the accession numbers P84105 for arenicin-1 and P84106 for arenicin-2.1were determined for each isoform. Each arenicin has one disulfide bond (Cys3-Cys20). The total RNA was isolated from the lugworm coelomocytes, RT-PCR and cloning were performed, and cDNA was sequenced. A 202-residue preproarenicin contains a putative signal peptide (25 amino acids) and a long prodomain. Arenicins have no structure similarity to any previously identified antimicrobial peptides. © 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

Ovchinnikova TV, Aleshina GM, Balandin SV, Krasnosdembskaya AD, Markelov ML, Frolova EI, Leonova YF, Tagaev AA, Krasnodembsky EG, Kokryakov VN

IBCH: 5108
Ссылка на статью в журнале: http://doi.wiley.com/10.1016/j.febslet.2004.10.012
Кол-во цитирований на 11.2023: 126
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