title: Solution structure of termite-derived antimicrobial peptide, spinigerin, as determined in SDS micelle by NMR spectroscopy.
abstract: Spinigerin is a linear antibacterial peptide derived from a termite insect. It consists of 25 amino acids and is devoid of cysteines. Spinigerin displays good lytic activities against Gram-positive and Gram-negative bacteria, but has no hemolytic activities against human erythrocytes. In this study, we present a three-dimensional solution structure of spinigerin in SDS micelles. According to CD data spinigerin has an alpha-helical conformation in the presence of TFE, DPC micelles, and SDS micelles. The three-dimensional structure of spinigerin as determined by NMR spectroscopy contains a stable alpha-helix from Lys4 to Thr23. Spinigerin (4-21), an 18-residue fragment from Lys4 to Leu21, contains a similar content of alpha-helical structure compared to native spinigerin and was found to retain antibacterial activity, too. Therefore, this alpha-helical structure and the strong electrostatic attraction between four Lys and three Arg residues in spinigerin and the negatively charged polar head groups of the phospholipids on the membrane surface play important roles in disrupting membrane and subsequent cell death.
authors.affiliation: Department of Chemistry, Konkuk University, Seoul 143-701, South Korea.
authors.forename: Kwang Hwan
authors.initials: KH
authors.lastname: Lee
authors.forename: Song Yub
authors.initials: SY
authors.lastname: Shin
authors.forename: Jung Eun
authors.initials: JE
authors.lastname: Hong
authors.forename: Sung-Tae
authors.initials: ST
authors.lastname: Yang
authors.forename: Jae Il
authors.initials: JI
authors.lastname: Kim
authors.forename: Kyung-Soo
authors.initials: KS
authors.lastname: Hahm
authors.forename: Yangmee
authors.initials: Y
authors.lastname: Kim
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides; D002942:Circular Dichroism; D006461:Hemolysis; D006801:Humans; D020049:Isoptera / Q000737:chemistry; D008081:Liposomes; D008823:Micelles; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides; D010743:Phospholipids; D011487:Protein Conformation; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry; D013329:Structure-Activity Relationship
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D008081:Liposomes; D008823:Micelles; D010455:Peptides; D010743:Phospholipids; C428303:spinigerin; D012967:Sodium Dodecyl Sulfate