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Evaluation of antimicrobial and anticancer activities of three peptides identified from the skin secretion of Hylarana latouchii

查看全文 作  者:Yan [1,2]Lin;Tianxing [1]Lin;Ningna [1]Cheng;Shuting [3]Wu;Jiancai [3]Huang;Xiaoling [2]Chen;Tianbao [2]Chen;Mei [2]Zhou;Lei [2]Wang;Chris [2]Shaw 高影响力作者 机构地区:[1]College of Animal Sciences(College of Bee Science),Fujian Agriculture and Forestry University,Fuzhou 350002,China;[2]Natural Drug Discovery Group,School of Pharmacy,Queen’s University,Belfast BT97BL,UK;[3]College of Chemistry,Fuzhou University,Fuzhou 350108,China高影响力机构 出  处:《Acta Biochimica et Biophysica Sinica》索引2021年第53卷第11期,共15页高影响力期刊 基  金:This work was supported by the grants from the Natural Science Foundation of Fujian Province(No.2019J01408);the Outstanding Young Scientist Program of Fujian Agriculture and Forestry University(No.xjq201916);the National Natural Science Foundation of China(No.31500753). 摘  要:The skins of frogs of the family Ranidae are particularly rich sources of biologically active peptides, among which antimicrobial peptides (AMPs) constitute the major portion. Some of these have attracted the interest of researchers because they possess both antimicrobial and anticancer activities. In this study, with ‘shotgun’ cloning & MS/MS fragmentation, three AMPs, homologues of family brevinin-1 (brevinin-1HL), & temporin (temporin-HLa and temporin-HLb), were discovered from the skin secretion of the broad-folded frog, Hylarana latouchii. They exhibited various degrees of antimicrobial & antibiofilm activities against test microorganisms & hemolysis on horse erythrocytes. It was found that they could induce bacteria death through disrupting cell membranes & binding to bacterial DNA. In addition, they also showed different potencies towards human cancer cell lines. The secondary structure & physicochemical properties of each peptide were investigated to preliminarily reveal their structure–activity relationships. Circular dichroism spectrometry showed that they all adopted a canonical α-helical conformation in membrane-mimetic solvents. Notably, the prepropeptide of brevinin-1HL from H. latouchii was highly identical to that of brevinin-1GHd from Hylarana guentheri, indicating a close relationship between these two species. Accordingly, this study provides candidates for the design of novel anti-infective & antineoplastic agents to fight multidrug-resistant bacteria & malignant tumors & also offers additional clues for the taxonomy of ranid frogs. 关 键 词:CLONING CHROMATOGRAPHY mass spectrometry structure-activity relationships
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