Solution Structures and Biological Functions of the Antimicrobial Peptide, Arenicin-1, and Its Linear Derivative.
From: Department of Bioscience and Biotechnology, Bio/Molecular Informatics Center, IBST, Konkuk University, Seoul, Korea.
Biopolymers
- Publish Date: 2007
- ISSN: 0006-3525
- Volume: 88
- Issue: 2
- Pages: 208-16
- Medium: Print
- Language: English
- Citation (JAMA): Lee Ju-Un, Kang Dong-Il, Zhu Wan Long, et al. Solution Structures and Biological Functions of the Antimicrobial Peptide, Arenicin-1, and Its Linear Derivative.. Biopolymers 2007;88:208-16
Abstract
Arenicin-1 (AR-1) is a novel antimicrobial peptide that was isolated from coelomocytes of the marine polychaeta lugworm Arenicola marina and shown to contain a single disulfide bond between Cys3 and Cys20, forming an 18-residue ring [Ovchinnikova, T. V. et al., FEBS Lett 2004, 577, 209-214]. To determine the role of this disulfide bond, we synthesized AR-1 (RWCVYAYVRVRGVLVRYRRCW) and its linear derivative, arenicin-1-S (AR-1-S: RWSVYAYVRVRGVLVRYRRSW). Activity assays revealed that AR-1-S is somewhat less active against bacterial cells than AR-1. Both peptides were very hydrophobic, and displayed cytotoxicity against human red blood cells. Analysis of the tertiary structures of AR-1 and AR-1-S by NMR spectroscopy disclosed that AR-1 has two-stranded antiparallel beta-sheet structures with amphipathicity, while AR-1-S displays a random coil structure in DMSO. Our biological data for AR-1 and AR-1-S indicate that the hydrophobic-hydrophilic balance, disulfide bridge, and the amphipathic beta-sheet structure of the peptides play important roles in their biological activities. Elucidation of the structure of AR-1 and its derivative should facilitate the design of novel non-cytotoxic peptide antibiotics with potent antibacterial activities.
Mesh Headings (Keywords): Amino Acid Sequence, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Bacteria, Hemolysis, Humans, Models, Molecular, Molecular Sequence Data, Molecular Structure, Nuclear Magnetic Resonance, Biomolecular, Peptides
Check for Full Text / PubMed Unique Identifier (PMID): 17285588
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