A Novel hybrid peptide Cecropin A(1-8)-LL37(17-30)with great Antibacterial Activity
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- 英文论文题名：A Novel hybrid peptide Cecropin A(1-8)-LL37(17-30)with great Antibacterial Activity
- 论文作者：Xubiao Wei ; Dayong Si ; Zhaojun Zheng ; Lulu Zhang ; Rujuan Wu ; Rijun Zhang
- 英文论文作者：Xubiao Wei ; Dayong Si ; Zhaojun Zheng ; Lulu Zhang ; Rujuan Wu ; Rijun Zhang ; Laboratory of Feed Biotechnology ; State Key Laboratory of Animal Nutrition ; College of Animal Science and Technology ; China Agricultural University
- 年：2016
- 作者机构：Laboratory of Feed Biotechnology,State Key Laboratory of Animal Nutrition,College of Animal Science and Technology,China Agricultural University;
- 英文论文关键词：hybrid peptide ; Cecropin A(1-8)-LL-37(17-30) ; antibacterial activity ; hemolytic activity
- 会议召开时间：2016-11-04
- 会议录名称：中国畜牧兽医学会动物微生态学分会第五届第十二次全国学术研讨会论文集
- 语种：英文
- 分类号：S816
- 学会代码：ZGXJ
- 会议名称：中国畜牧兽医学会动物微生态学分会第五届第十二次全国学术研讨会
- 会议地点：中国山东青岛
- 主办单位：中国畜牧兽医学会动物微生态学分会
- 学会名称：中国畜牧兽医学会
- 页数：1
- 文件大小：61k
- 原文格式：O
- 会议级别：全国
摘要
Antimicrobial peptides are attracting more attention as a therapeutic alternative compared to traditional antibiotics in the field of disease control and prevention due to their unique mechanism of action and broad spectrum antimicrobial activity.LL-37(L),a linear helical peptide isolated from human leukocytes and epithelia,plays a critical role in the process of antimicrobial infection,angiogenesis,wound healing and apoptosis[1].However,it shows undesirable hemolytic activity against eukaryotic cells by inducing membrane disruption,which largely limits its application in clinic[2].Cecropin A(C),a antibacterial peptide produced by Hyalophora cecropia,shows broad bioactivities such as antibacterial,anti-inflammation and anticancer,but it does not lyses eukaryotic cells[3,4].In our study,the hybrid peptide C(1-8)-L(17-30)(C-L) was designed by combining the N-terminal amphipathic α-helix fragment of C with the core antimicrobial fragment of L on the basis of the hypothesis that the combination will elevate the antimicrobial property and minimize the hemolytic activity.Results showed that the antibacterial property of C-L was greatly improved when compared to parental peptides,and C-L did not show cytotoxicity in comparison with L.Moreover,C-L was better than C and L in sterilization speed and efficacy.In sum,this research not only supplied an effective approach for acquiring excellent hybrid peptide C-L,but pave the way for its further exploration on pharmaceutical and medical importance.
Antimicrobial peptides are attracting more attention as a therapeutic alternative compared to traditional antibiotics in the field of disease control and prevention due to their unique mechanism of action and broad spectrum antimicrobial activity.LL-37(L),a linear helical peptide isolated from human leukocytes and epithelia,plays a critical role in the process of antimicrobial infection,angiogenesis,wound healing and apoptosis[1].However,it shows undesirable hemolytic activity against eukaryotic cells by inducing membrane disruption,which largely limits its application in clinic[2].Cecropin A(C),a antibacterial peptide produced by Hyalophora cecropia,shows broad bioactivities such as antibacterial,anti-inflammation and anticancer,but it does not lyses eukaryotic cells[3,4].In our study,the hybrid peptide C(1-8)-L(17-30)(C-L) was designed by combining the N-terminal amphipathic α-helix fragment of C with the core antimicrobial fragment of L on the basis of the hypothesis that the combination will elevate the antimicrobial property and minimize the hemolytic activity.Results showed that the antibacterial property of C-L was greatly improved when compared to parental peptides,and C-L did not show cytotoxicity in comparison with L.Moreover,C-L was better than C and L in sterilization speed and efficacy.In sum,this research not only supplied an effective approach for acquiring excellent hybrid peptide C-L,but pave the way for its further exploration on pharmaceutical and medical importance.
Antimicrobial peptides are attracting more attention as a therapeutic alternative compared to traditional antibiotics in the field of disease control and prevention due to their unique mechanism of action and broad spectrum antimicrobial activity.LL-37(L),a linear helical peptide isolated from human leukocytes and epithelia,plays a critical role in the process of antimicrobial infection,angiogenesis,wound healing and apoptosis[1].However,it shows undesirable hemolytic activity against eukaryotic cells by inducing membrane disruption,which largely limits its application in clinic[2].Cecropin A(C),a antibacterial peptide produced by Hyalophora cecropia,shows broad bioactivities such as antibacterial,anti-inflammation and anticancer,but it does not lyses eukaryotic cells[3,4].In our study,the hybrid peptide C(1-8)-L(17-30)(C-L) was designed by combining the N-terminal amphipathic α-helix fragment of C with the core antimicrobial fragment of L on the basis of the hypothesis that the combination will elevate the antimicrobial property and minimize the hemolytic activity.Results showed that the antibacterial property of C-L was greatly improved when compared to parental peptides,and C-L did not show cytotoxicity in comparison with L.Moreover,C-L was better than C and L in sterilization speed and efficacy.In sum,this research not only supplied an effective approach for acquiring excellent hybrid peptide C-L,but pave the way for its further exploration on pharmaceutical and medical importance.
引文
[1]D.Vandamme,B.Landuyt,W.Luyten,L.Schoofs,A comprehensive summary of LL-37,the factotum human cathelicidin peptide.CELL IMMUNOL 280(2012)22-35.
[2]R.Ramos,J.R Silva,A.C.Rodrigues,R.Costa,L.Guardao,F.Schmitt,R.Soares,M.Vilanova,L.Domingues,M.Gama,Wound healing activity of the human antimicrobial peptide LL37.PEPTIDES 32(2011)1469-1476.
[3]D.W.Hoskin,A.Ramamoorthy,Studies on anticancer activities of antimicrobial peptides.Biochim Biophys Acta1778(2008)357-375.
[4]A.Giacometti,O.Cirioni,W.Kamysz,G.D'Amato,C.Silvestri,M.S.Del Prete,J.Lukasiak,G.Scalise,Comparative activities of cecropin A,melittin,and cecropin A-melittin peptide CA(1-7)M(2-9)NH2 against multidrag-resistant nosocomial isolates of Acinetobacter baumannii.PEPTIDES 24(2003)1315-1318
[2]R.Ramos,J.R Silva,A.C.Rodrigues,R.Costa,L.Guardao,F.Schmitt,R.Soares,M.Vilanova,L.Domingues,M.Gama,Wound healing activity of the human antimicrobial peptide LL37.PEPTIDES 32(2011)1469-1476.
[3]D.W.Hoskin,A.Ramamoorthy,Studies on anticancer activities of antimicrobial peptides.Biochim Biophys Acta1778(2008)357-375.
[4]A.Giacometti,O.Cirioni,W.Kamysz,G.D'Amato,C.Silvestri,M.S.Del Prete,J.Lukasiak,G.Scalise,Comparative activities of cecropin A,melittin,and cecropin A-melittin peptide CA(1-7)M(2-9)NH2 against multidrag-resistant nosocomial isolates of Acinetobacter baumannii.PEPTIDES 24(2003)1315-1318