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Synthesis and antimicrobial activity of cysteine-free coprisin nonapeptides.
Lee, Jaeho; Lee, Daeun; Choi, Hyemin; Kim, Ha Hyung; Kim, Ho; Hwang, Jae Sam; Lee, Dong Gun; Kim, Jae Il.
Afiliación
  • Lee J; School of Life Sciences, Gwangju Institute of Science and Technology, Oryong-dong, Buk-gu, Gwangju 500-712, Republic of Korea.
  • Lee D; School of Life Sciences, Gwangju Institute of Science and Technology, Oryong-dong, Buk-gu, Gwangju 500-712, Republic of Korea.
  • Choi H; School of Life Sciences and Biotechnology, College of Natural Sciences, Kyungpook National University, Daehak-ro 80, Buk-gu, Daegu 702-701, Republic of Korea.
  • Kim HH; College of Pharmacy, Chung-Ang University, Seoul, Republic of Korea.
  • Kim H; School of Life Sciences and Biotechnology, College of Natural Science, Daejin University, Pocheon, Gyeonggido, Republic of Korea.
  • Hwang JS; Department of Agricultural Biology, Natural Academy of Agricultural Science, RDA, Suwon 441-853, Republic of Korea.
  • Lee DG; School of Life Sciences and Biotechnology, College of Natural Sciences, Kyungpook National University, Daehak-ro 80, Buk-gu, Daegu 702-701, Republic of Korea.
  • Kim JI; School of Life Sciences, Gwangju Institute of Science and Technology, Oryong-dong, Buk-gu, Gwangju 500-712, Republic of Korea. Electronic address: jikim@gist.ac.kr.
Biochem Biophys Res Commun ; 443(2): 483-8, 2014 Jan 10.
Article en En | MEDLINE | ID: mdl-24321546
Coprisin is a 43-mer defensin-like peptide from the dung beetle, Copris tripartitus. CopA3 (LLCIALRKK-NH2), a 9-mer peptide containing a single free cysteine residue at position 3 of its sequence, was derived from the α-helical region of coprisin and exhibits potent antibacterial and anti-inflammatory activities. The single cysteine implies a tendency for dimerization; however, it remains unknown whether this cysteine residue is indispensible for CopA3's antimicrobial activity. To address this issue, in the present study we synthesized eight cysteine-substituted monomeric CopA3 analogs and two dimeric analogs, CopA3 (Dimer) and CopIK (Dimer), and evaluated their antimicrobial effects against bacteria and fungi, as well as their hemolytic activity toward human erythrocytes. Under physiological conditions, CopA3 (Mono) exhibits a 6/4 (monomer/dimer) molar ratio in HPLC area percent, indicating that its effects on bacterial strains likely reflect a CopA3 (Mono)/CopA3 (Dimer) mixture. We also report the identification of CopW, a new cysteine-free nonapeptide derived from CopA3 that has potent antimicrobial activity with virtually no hemolytic activity. Apparently, the cysteine residue in CopA3 is not essential for its antimicrobial function. Notably, CopW also exhibited significant synergistic activity with ampicillin and showed more potent antifungal activity than either wild-type coprisin or melittin.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Bacterias / Fenómenos Fisiológicos Bacterianos / Proteínas de Insectos / Cisteína / Hongos Idioma: En Revista: Biochem Biophys Res Commun Año: 2014 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Bacterias / Fenómenos Fisiológicos Bacterianos / Proteínas de Insectos / Cisteína / Hongos Idioma: En Revista: Biochem Biophys Res Commun Año: 2014 Tipo del documento: Article Pais de publicación: Estados Unidos