Development of a novel antimicrobial peptide AWRK6

被引:10
作者
Kim, Dusik [1 ]
Wang, Zheng [2 ]
Jin, Lili [2 ]
Li, Hanpin [2 ]
Hwang, Junwei [1 ]
Hanrahan, John W. [1 ]
Wang, Qiuyu [3 ]
机构
[1] McGill Univ, Dept Physiol, 3655 Drummond St, Montreal, PQ H3G 1Y6, Canada
[2] Liaoning Univ, Life Sicience Sch, Shenyang 110036, Peoples R China
[3] Res Ctr Comp Simulating & Informat Proc Biomacrom, Shenyang 110036, Peoples R China
关键词
CHINESE FROG; SKIN; HYDROPHOBICITY; IDENTIFICATION; CONFORMATION; ANTIBIOTICS; TRITRPTICIN; BACTERIA; DEFENSE;
D O I
10.3329/bjp.v11i2.25031
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
We have previously identified an antimicrobial peptide called dybowskin2-CDYa (Dy2) in the cutaneous secretion from the Chinese frog Rana dybowskii. In this study, we used Dy2 as a template to prepare some novel peptides with improved stability and hydrophobicity. The antimicrobial activities exerted by these peptides against Gram positive and Gram negative bacteria were evaluated by MIC and CFU assays under physiological conditions. One peptide, AWRK6, was 2-4 fold more potent than Dy2, and was toxic to most of the bacterial strains tested, exhibiting a faster killing rate. AWRK6 was most potent in alkaline environments, and this was related to the more highly organized secondary structure of the peptide, as revealed by circular dichroism spectroscopy. Furthermore, AWRK6 was more resistant than Dy2 to degradation by trypsin. The improved properties of AWRK6 suggested that the peptide could potentially be further developed into an antibiotic.
引用
收藏
页码:460 / 468
页数:9
相关论文
共 24 条
  • [1] Afacan NJ, 2012, CURR PHARM DESIGN, V18, P807, DOI 10.2174/138161212799277617
  • [2] Structure-activity relationship of indolicidin, a Trp-rich antibacterial peptide
    Ando, Setsuko
    Mitsuyasu, Keitarou
    Soeda, Yoshitake
    Hidaka, Mariko
    Ito, Yuki
    Matsubara, Kouki
    Shindo, Mitsuno
    Uchida, Yoshiki
    Aoyagi, Haruhiko
    [J]. JOURNAL OF PEPTIDE SCIENCE, 2010, 16 (04) : 171 - 177
  • [3] PEPTIDE ANTIBIOTICS AND THEIR ROLE IN INNATE IMMUNITY
    BOMAN, HG
    [J]. ANNUAL REVIEW OF IMMUNOLOGY, 1995, 13 : 61 - 92
  • [4] Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    Brogden, KA
    [J]. NATURE REVIEWS MICROBIOLOGY, 2005, 3 (03) : 238 - 250
  • [5] NPS@:: Network Protein Sequence Analysis
    Combet, C
    Blanchet, C
    Geourjon, C
    Deléage, G
    [J]. TRENDS IN BIOCHEMICAL SCIENCES, 2000, 25 (03) : 147 - 150
  • [6] Conlon JM, 2010, METHODS MOL BIOL, V618, P3, DOI 10.1007/978-1-60761-594-1_1
  • [7] REDESIGNING TRYPSIN - ALTERATION OF SUBSTRATE-SPECIFICITY
    CRAIK, CS
    LARGMAN, C
    FLETCHER, T
    ROCZNIAK, S
    BARR, PJ
    FLETTERICK, R
    RUTTER, WJ
    [J]. SCIENCE, 1985, 228 (4697) : 291 - 297
  • [8] In vitro susceptibility tests for cationic peptides: Comparison of broth microdilution methods for bacteria that grow aerobically
    Giacometti, A
    Cirioni, O
    Barchiesi, F
    Del Prete, MS
    Fortuna, M
    Caselli, F
    Scalise, G
    [J]. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 2000, 44 (06) : 1694 - 1696
  • [9] Identification and characterisation of a novel antimicrobial polypeptide from the skin secretion of a Chinese frog (Rana chensinensis)
    Jin, Li L.
    Song, Shu S.
    Li, Qiang
    Chen, Yu H.
    Wang, Qiu Y.
    Hou, Sheng T.
    [J]. INTERNATIONAL JOURNAL OF ANTIMICROBIAL AGENTS, 2009, 33 (06) : 538 - 542
  • [10] Characterization of antimicrobial peptides isolated from the skin of the Chinese frog, Rana dybowskii
    Jin, Li-Li
    Li, Qiang
    Song, Shu-Sen
    Feng, Kai
    Zhang, Dian-Bao
    Wang, Qiu-Yu
    Chen, Yu-Hua
    [J]. COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, 2009, 154 (02): : 174 - 178