{"title":"含有人Ll37 Cathelecidin短段非活性Iv13序列的杂联肽Tat-IV13的抑菌和抗癌特性","authors":"Alphonse Garcia, B. Périchon","doi":"10.31487/j.cmr.2019.01.03","DOIUrl":null,"url":null,"abstract":"Therapeutic strategies based on optimization of the unique human LL37 cathelecin sequences including FK16, the core active sequence of LL37, have already been proposed. In this study we have characterized TatIV13 a new host defense hybrid peptide, that combined YGRRKKRRQRRR, the hydrophobic N-terminal\nfragment of HIV-1 Tat47-57 cell penetrating sequence, with IV13, a short IVQRIKDFLRNLV inactive\nsequence resulting from the deletion of the three N-terminal amino acid residues of FK16. Tat- IV13\ndisplayed potent host defense inhibitory effects leading both to the survival inhibition of U87G cells, a\nglioblastoma model, and to the inhibition of the growth of S. agalactiae NEM316 ΔdltA strain, a Gram+\nbacterial model. These results suggest that identification of hybrid specific Tat-cathelecidin peptides with\nhigh anti-tumor activity and anti-bactericidal activity may represent a powerful approach to identify new\ncandidates for future therapeutic developments.\n","PeriodicalId":364792,"journal":{"name":"Clinical Microbiology and Research","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2019-12-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Anti-Microbial and Anti-Cancer Properties of Tat-IV13, A Hybrid Bi-Partite Peptide Containing The Short Non Active Iv13 Sequence of Human Ll37 Cathelecidin\",\"authors\":\"Alphonse Garcia, B. Périchon\",\"doi\":\"10.31487/j.cmr.2019.01.03\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Therapeutic strategies based on optimization of the unique human LL37 cathelecin sequences including FK16, the core active sequence of LL37, have already been proposed. In this study we have characterized TatIV13 a new host defense hybrid peptide, that combined YGRRKKRRQRRR, the hydrophobic N-terminal\\nfragment of HIV-1 Tat47-57 cell penetrating sequence, with IV13, a short IVQRIKDFLRNLV inactive\\nsequence resulting from the deletion of the three N-terminal amino acid residues of FK16. Tat- IV13\\ndisplayed potent host defense inhibitory effects leading both to the survival inhibition of U87G cells, a\\nglioblastoma model, and to the inhibition of the growth of S. agalactiae NEM316 ΔdltA strain, a Gram+\\nbacterial model. These results suggest that identification of hybrid specific Tat-cathelecidin peptides with\\nhigh anti-tumor activity and anti-bactericidal activity may represent a powerful approach to identify new\\ncandidates for future therapeutic developments.\\n\",\"PeriodicalId\":364792,\"journal\":{\"name\":\"Clinical Microbiology and Research\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2019-12-05\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Clinical Microbiology and Research\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.31487/j.cmr.2019.01.03\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Clinical Microbiology and Research","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.31487/j.cmr.2019.01.03","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Anti-Microbial and Anti-Cancer Properties of Tat-IV13, A Hybrid Bi-Partite Peptide Containing The Short Non Active Iv13 Sequence of Human Ll37 Cathelecidin
Therapeutic strategies based on optimization of the unique human LL37 cathelecin sequences including FK16, the core active sequence of LL37, have already been proposed. In this study we have characterized TatIV13 a new host defense hybrid peptide, that combined YGRRKKRRQRRR, the hydrophobic N-terminal
fragment of HIV-1 Tat47-57 cell penetrating sequence, with IV13, a short IVQRIKDFLRNLV inactive
sequence resulting from the deletion of the three N-terminal amino acid residues of FK16. Tat- IV13
displayed potent host defense inhibitory effects leading both to the survival inhibition of U87G cells, a
glioblastoma model, and to the inhibition of the growth of S. agalactiae NEM316 ΔdltA strain, a Gram+
bacterial model. These results suggest that identification of hybrid specific Tat-cathelecidin peptides with
high anti-tumor activity and anti-bactericidal activity may represent a powerful approach to identify new
candidates for future therapeutic developments.