Piyachat Wiriyaampaiwong, Chutima Karnmongkol, Arpaporn Punpad, Nattapong Srisamoot, Wutti Rattanavichai, Alongkod Tanomtong, S. Daduang, S. Klaynongsruang, A. Tankrathok
{"title":"Cathelicidin-HR from Hoplobatrachus rugulosus: an antioxidant peptide that performs a protective effect against UV/H2O2 -induced DNA damage","authors":"Piyachat Wiriyaampaiwong, Chutima Karnmongkol, Arpaporn Punpad, Nattapong Srisamoot, Wutti Rattanavichai, Alongkod Tanomtong, S. Daduang, S. Klaynongsruang, A. Tankrathok","doi":"10.7324/jabb.2022.100405","DOIUrl":null,"url":null,"abstract":"Cathelicidins, a group of vertebrate multifunctional molecules, play a role in innate immunity. In this study, a cathelicidin was identified from the lungs of frogs, Hoplobatrachus rugulosus . A 474 base pairs complementary DNA sequence encoded a 157 amino acid residue prepropeptide of H. rugulosus cathelicidin (cathelicidin-HR), which consisting of a 20-residue signal peptide sequence, a 108-residue cathelin region, and a 29-residue cathelicidin-HR peptide. Amino acid sequence alignment and cladogram analysis illustrated that cathelicidin-HR have a high degree of similarity to other amphibian cathelicidins. The cathelicidin-HR peptide displays very low antimicrobial activity but exhibits dose-dependent antioxidant activity. Moreover, this peptide expresses DNA damage inhibition against UV/H 2 O 2 -induction. The molecular docking indicated that DNA damage protection of cathelicidin-HR might occur via DNA-peptide complex formation. This is the first amphibian cathelicidin peptide that possesses DNA damage inhibitory activity which might play a crucial role in oxidative stress.","PeriodicalId":423079,"journal":{"name":"Journal of Applied Biology & Biotechnology","volume":"52 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2022-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Applied Biology & Biotechnology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.7324/jabb.2022.100405","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Cathelicidins, a group of vertebrate multifunctional molecules, play a role in innate immunity. In this study, a cathelicidin was identified from the lungs of frogs, Hoplobatrachus rugulosus . A 474 base pairs complementary DNA sequence encoded a 157 amino acid residue prepropeptide of H. rugulosus cathelicidin (cathelicidin-HR), which consisting of a 20-residue signal peptide sequence, a 108-residue cathelin region, and a 29-residue cathelicidin-HR peptide. Amino acid sequence alignment and cladogram analysis illustrated that cathelicidin-HR have a high degree of similarity to other amphibian cathelicidins. The cathelicidin-HR peptide displays very low antimicrobial activity but exhibits dose-dependent antioxidant activity. Moreover, this peptide expresses DNA damage inhibition against UV/H 2 O 2 -induction. The molecular docking indicated that DNA damage protection of cathelicidin-HR might occur via DNA-peptide complex formation. This is the first amphibian cathelicidin peptide that possesses DNA damage inhibitory activity which might play a crucial role in oxidative stress.