N. Bernardes, A. Ribeiro, R. Seruca, J. Paredes, A. Fialho
{"title":"Bacterial protein azurin as a new candidate drug to treat untreatable breast cancers","authors":"N. Bernardes, A. Ribeiro, R. Seruca, J. Paredes, A. Fialho","doi":"10.1109/ENBENG.2011.6026047","DOIUrl":null,"url":null,"abstract":"Azurin is a blue copper protein produced by Pseudomonas aeruginosa. Azurin enters preferentially into cancer cells and forms a complex with p53, stabilizing it and inducing apoptosis. Azurin allows in vivo regression of human melanoma and breast cancer without toxic effects to the animal. Its immunoglobulin-like fold and a large exposed hydrophobic patch confer on it the property of a natural scaffold. This has already been proven for the receptor tyrosine kinase EphB2, since azurin prevents its binding to the ligand ephrinB2. We intend to extend the azurin interaction to cell adhesion molecules (CAMs), particularly P-cadherin. P-cadherin is frequently overexpressed in invasive breast carcinomas and it is a poor prognosis marker. Protein-protein docking results have validated this approach confirming an interaction between both proteins. Thus, natural azurin or derived proteins or peptides could be scaffolds against these proteins in breast cancer cells models, being an interesting new therapeutic tool.","PeriodicalId":206538,"journal":{"name":"1st Portuguese Biomedical Engineering Meeting","volume":"47 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2011-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"6","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"1st Portuguese Biomedical Engineering Meeting","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1109/ENBENG.2011.6026047","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 6
Abstract
Azurin is a blue copper protein produced by Pseudomonas aeruginosa. Azurin enters preferentially into cancer cells and forms a complex with p53, stabilizing it and inducing apoptosis. Azurin allows in vivo regression of human melanoma and breast cancer without toxic effects to the animal. Its immunoglobulin-like fold and a large exposed hydrophobic patch confer on it the property of a natural scaffold. This has already been proven for the receptor tyrosine kinase EphB2, since azurin prevents its binding to the ligand ephrinB2. We intend to extend the azurin interaction to cell adhesion molecules (CAMs), particularly P-cadherin. P-cadherin is frequently overexpressed in invasive breast carcinomas and it is a poor prognosis marker. Protein-protein docking results have validated this approach confirming an interaction between both proteins. Thus, natural azurin or derived proteins or peptides could be scaffolds against these proteins in breast cancer cells models, being an interesting new therapeutic tool.