Géssica Gomes Barbosa , Carlos José Correia de Santana , Tulíbia Laurindo Silva , Brenda Conceição Guimarães Santana , Patrícia Maria Guedes Paiva , Gabriel Gonçalves de Freitas , Guilherme Dotto Brand , Osmindo Rodrigues Pires Júnior , Mariana S. Castro , Thiago Henrique Napoleão
{"title":"来自巴西大西洋森林的 Lithobates palmipes (Spix, 1824) (Amphibia: Ranidae) 皮肤分泌物的一种具有抗菌活性和细胞毒性的新颞素。","authors":"Géssica Gomes Barbosa , Carlos José Correia de Santana , Tulíbia Laurindo Silva , Brenda Conceição Guimarães Santana , Patrícia Maria Guedes Paiva , Gabriel Gonçalves de Freitas , Guilherme Dotto Brand , Osmindo Rodrigues Pires Júnior , Mariana S. Castro , Thiago Henrique Napoleão","doi":"10.1016/j.cbpb.2024.111041","DOIUrl":null,"url":null,"abstract":"<div><div>This work investigated the peptide profile of skin secretion from <em>Lithobates palmipes</em> collected from the Brazilian Atlantic Forest. The secretion was submitted to reversed phase high-performance liquid chromatography (RP-HPLC) and the fractions were screened for antibacterial activity. RP-HPLC resulted in the separation of several peaks, among which 10 showed antibacterial activity and contained peptides of the ranatuerin, brevinin and temporin families. Fraction 6 was resubmitted to RP-HPLC and a novel peptide from temporin family (temporin-PMb) had its primary structure determined. Temporin-PMb and non-amidated temporin-PMb were synthesized, purified, and evaluated for antibacterial activity, hemolytic activity and cytotoxicity to keratinocytes and cancer cells. Temporin-PMb was active against <em>Klebsiella pneumoniae</em>, <em>Staphylococcus aureus</em>, <em>Escherichia coli</em>, and <em>Pseudomonas aeruginosa</em> as well as against methicilin-resistant <em>S. aureus</em> (MRSA) and <em>Acinetobacter baumannii</em>. It was cytotoxic to human cervical adenocarcinoma cells (HeLa) and human mammary adenocarcinoma cells (MCF7) with IC<sub>50</sub> of 32.4 and 24.1 μM, respectively. It was also toxic to human keratinocytes (HaCaT; IC<sub>50</sub> of 25.0 μM) and showed hemolytic activity. The non-amidated form showed low hemolytic activity and lower HaCaT toxicity, but was only effective against <em>E. coli</em>, <em>S. aureus</em> MRSA, and <em>A. baumanii</em>. In conclusion, Atlantic Forest <em>L. palmipes</em> skin secretion contained different bioactive peptides, including a novel temporin with antibacterial effect and cytotoxicity towards human cancer cells. The amide group was responsible for the activities of the wild-type temporin-PMb. Peptide engineering studies are encouraged aiming at minimizing unwanted effects.</div></div>","PeriodicalId":1,"journal":{"name":"Accounts of Chemical Research","volume":null,"pages":null},"PeriodicalIF":16.4000,"publicationDate":"2024-10-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"A new temporin with antibacterial activity and cytotoxicity from the skin secretion of Lithobates palmipes (Spix, 1824) (Amphibia: Ranidae) from Brazilian Atlantic Forest\",\"authors\":\"Géssica Gomes Barbosa , Carlos José Correia de Santana , Tulíbia Laurindo Silva , Brenda Conceição Guimarães Santana , Patrícia Maria Guedes Paiva , Gabriel Gonçalves de Freitas , Guilherme Dotto Brand , Osmindo Rodrigues Pires Júnior , Mariana S. Castro , Thiago Henrique Napoleão\",\"doi\":\"10.1016/j.cbpb.2024.111041\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>This work investigated the peptide profile of skin secretion from <em>Lithobates palmipes</em> collected from the Brazilian Atlantic Forest. The secretion was submitted to reversed phase high-performance liquid chromatography (RP-HPLC) and the fractions were screened for antibacterial activity. RP-HPLC resulted in the separation of several peaks, among which 10 showed antibacterial activity and contained peptides of the ranatuerin, brevinin and temporin families. Fraction 6 was resubmitted to RP-HPLC and a novel peptide from temporin family (temporin-PMb) had its primary structure determined. Temporin-PMb and non-amidated temporin-PMb were synthesized, purified, and evaluated for antibacterial activity, hemolytic activity and cytotoxicity to keratinocytes and cancer cells. Temporin-PMb was active against <em>Klebsiella pneumoniae</em>, <em>Staphylococcus aureus</em>, <em>Escherichia coli</em>, and <em>Pseudomonas aeruginosa</em> as well as against methicilin-resistant <em>S. aureus</em> (MRSA) and <em>Acinetobacter baumannii</em>. It was cytotoxic to human cervical adenocarcinoma cells (HeLa) and human mammary adenocarcinoma cells (MCF7) with IC<sub>50</sub> of 32.4 and 24.1 μM, respectively. It was also toxic to human keratinocytes (HaCaT; IC<sub>50</sub> of 25.0 μM) and showed hemolytic activity. The non-amidated form showed low hemolytic activity and lower HaCaT toxicity, but was only effective against <em>E. coli</em>, <em>S. aureus</em> MRSA, and <em>A. baumanii</em>. In conclusion, Atlantic Forest <em>L. palmipes</em> skin secretion contained different bioactive peptides, including a novel temporin with antibacterial effect and cytotoxicity towards human cancer cells. The amide group was responsible for the activities of the wild-type temporin-PMb. Peptide engineering studies are encouraged aiming at minimizing unwanted effects.</div></div>\",\"PeriodicalId\":1,\"journal\":{\"name\":\"Accounts of Chemical Research\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":16.4000,\"publicationDate\":\"2024-10-18\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Accounts of Chemical Research\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1096495924001088\",\"RegionNum\":1,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Accounts of Chemical Research","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1096495924001088","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
A new temporin with antibacterial activity and cytotoxicity from the skin secretion of Lithobates palmipes (Spix, 1824) (Amphibia: Ranidae) from Brazilian Atlantic Forest
This work investigated the peptide profile of skin secretion from Lithobates palmipes collected from the Brazilian Atlantic Forest. The secretion was submitted to reversed phase high-performance liquid chromatography (RP-HPLC) and the fractions were screened for antibacterial activity. RP-HPLC resulted in the separation of several peaks, among which 10 showed antibacterial activity and contained peptides of the ranatuerin, brevinin and temporin families. Fraction 6 was resubmitted to RP-HPLC and a novel peptide from temporin family (temporin-PMb) had its primary structure determined. Temporin-PMb and non-amidated temporin-PMb were synthesized, purified, and evaluated for antibacterial activity, hemolytic activity and cytotoxicity to keratinocytes and cancer cells. Temporin-PMb was active against Klebsiella pneumoniae, Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa as well as against methicilin-resistant S. aureus (MRSA) and Acinetobacter baumannii. It was cytotoxic to human cervical adenocarcinoma cells (HeLa) and human mammary adenocarcinoma cells (MCF7) with IC50 of 32.4 and 24.1 μM, respectively. It was also toxic to human keratinocytes (HaCaT; IC50 of 25.0 μM) and showed hemolytic activity. The non-amidated form showed low hemolytic activity and lower HaCaT toxicity, but was only effective against E. coli, S. aureus MRSA, and A. baumanii. In conclusion, Atlantic Forest L. palmipes skin secretion contained different bioactive peptides, including a novel temporin with antibacterial effect and cytotoxicity towards human cancer cells. The amide group was responsible for the activities of the wild-type temporin-PMb. Peptide engineering studies are encouraged aiming at minimizing unwanted effects.
期刊介绍：
Accounts of Chemical Research presents short, concise and critical articles offering easy-to-read overviews of basic research and applications in all areas of chemistry and biochemistry. These short reviews focus on research from the author’s own laboratory and are designed to teach the reader about a research project. In addition, Accounts of Chemical Research publishes commentaries that give an informed opinion on a current research problem. Special Issues online are devoted to a single topic of unusual activity and significance.
Accounts of Chemical Research replaces the traditional article abstract with an article "Conspectus." These entries synopsize the research affording the reader a closer look at the content and significance of an article. Through this provision of a more detailed description of the article contents, the Conspectus enhances the article's discoverability by search engines and the exposure for the research.
京公网安备 11010802042870号
京ICP备2023020795号-1
分享
求助内容：
应助结果提醒方式：
扫码关注我们
