{"title":"用治疗性共轭碳纳米管检测基质金属蛋白酶-14 (MMP-14) 的 PEX 类域。","authors":"D Vieira, J Barralet, E J Harvey, G Merle","doi":"10.3390/bios12100884","DOIUrl":null,"url":null,"abstract":"<p><p>Matrix metalloproteinases (MMPs) are essential proteins acting directly in the breakdown of the extra cellular matrix and so in cancer invasion and metastasis. Given its impact on tumor angiogenesis, monitoring MMP-14 provides strategic insights on cancer severity and treatment. In this work, we report a new approach to improve the electrochemical interaction of the MMP-14 with the electrode surface while preserving high specificity. This is based on the detection of the hemopexin (PEX) domain of MMP-14, which has a greater availability with a stable and low-cost commercial molecule, as a recognition element. This molecule, called NSC-405020, is specific of the PEX domain of MMP-14 within the binding pocket. Through the covalent grafting of the NSC-405020 molecule on carbon nanotubes (CNTs), we were able to detect and quantify MMP-14 using electrochemical impedance spectroscopy with a linear range of detection of 10 ng⋅mL<sup>-1</sup> to 100 ng⋅mL<sup>-1</sup>, and LOD of 7.5 ng⋅mL<sup>-1</sup>. The specificity of the inhibitory small molecule was validated against the PEX domain of MMP-1. The inhibitor loaded CNTs system showed as a desirable candidate to become an alternative to the conventional recognition bioelements for the detection of MMP-14.</p>","PeriodicalId":46981,"journal":{"name":"Journal of African Business","volume":"18 1","pages":""},"PeriodicalIF":2.1000,"publicationDate":"2022-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9599479/pdf/","citationCount":"0","resultStr":"{\"title\":\"Detecting the PEX Like Domain of Matrix Metalloproteinase-14 (MMP-14) with Therapeutic Conjugated CNTs.\",\"authors\":\"D Vieira, J Barralet, E J Harvey, G Merle\",\"doi\":\"10.3390/bios12100884\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Matrix metalloproteinases (MMPs) are essential proteins acting directly in the breakdown of the extra cellular matrix and so in cancer invasion and metastasis. Given its impact on tumor angiogenesis, monitoring MMP-14 provides strategic insights on cancer severity and treatment. In this work, we report a new approach to improve the electrochemical interaction of the MMP-14 with the electrode surface while preserving high specificity. This is based on the detection of the hemopexin (PEX) domain of MMP-14, which has a greater availability with a stable and low-cost commercial molecule, as a recognition element. This molecule, called NSC-405020, is specific of the PEX domain of MMP-14 within the binding pocket. Through the covalent grafting of the NSC-405020 molecule on carbon nanotubes (CNTs), we were able to detect and quantify MMP-14 using electrochemical impedance spectroscopy with a linear range of detection of 10 ng⋅mL<sup>-1</sup> to 100 ng⋅mL<sup>-1</sup>, and LOD of 7.5 ng⋅mL<sup>-1</sup>. The specificity of the inhibitory small molecule was validated against the PEX domain of MMP-1. The inhibitor loaded CNTs system showed as a desirable candidate to become an alternative to the conventional recognition bioelements for the detection of MMP-14.</p>\",\"PeriodicalId\":46981,\"journal\":{\"name\":\"Journal of African Business\",\"volume\":\"18 1\",\"pages\":\"\"},\"PeriodicalIF\":2.1000,\"publicationDate\":\"2022-10-17\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9599479/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of African Business\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://doi.org/10.3390/bios12100884\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BUSINESS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of African Business","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.3390/bios12100884","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BUSINESS","Score":null,"Total":0}
Detecting the PEX Like Domain of Matrix Metalloproteinase-14 (MMP-14) with Therapeutic Conjugated CNTs.
Matrix metalloproteinases (MMPs) are essential proteins acting directly in the breakdown of the extra cellular matrix and so in cancer invasion and metastasis. Given its impact on tumor angiogenesis, monitoring MMP-14 provides strategic insights on cancer severity and treatment. In this work, we report a new approach to improve the electrochemical interaction of the MMP-14 with the electrode surface while preserving high specificity. This is based on the detection of the hemopexin (PEX) domain of MMP-14, which has a greater availability with a stable and low-cost commercial molecule, as a recognition element. This molecule, called NSC-405020, is specific of the PEX domain of MMP-14 within the binding pocket. Through the covalent grafting of the NSC-405020 molecule on carbon nanotubes (CNTs), we were able to detect and quantify MMP-14 using electrochemical impedance spectroscopy with a linear range of detection of 10 ng⋅mL-1 to 100 ng⋅mL-1, and LOD of 7.5 ng⋅mL-1. The specificity of the inhibitory small molecule was validated against the PEX domain of MMP-1. The inhibitor loaded CNTs system showed as a desirable candidate to become an alternative to the conventional recognition bioelements for the detection of MMP-14.
期刊介绍:
Journal of African Business is the official journal of the Academy of African Business and Development, the largest network of professionals committed to advancement of business development in African nations. JAB strives to comprehensively cover all business disciplines by publishing high quality analytical, conceptual, and empirical articles that demonstrate a substantial contribution to the broad domain of African business. Regardless of the research context, tradition, approach, or philosophy, manuscripts submitted to JAB must demonstrate that the topics investigated are important to the understanding of business practices and the advancement of business knowledge in or with Africa. Particularly, JAB welcomes qualitative and quantitative research papers. JAB is not, however, limited to African-based empirical studies. It searches for various contributions, including those based on countries outside Africa that address issues relevant to African business. Targeted toward academics, policymakers, consultants, and executives, JAB features the latest theoretical developments and cutting-edge research that challenge established beliefs and paradigms and offer alternative ways to cope with the endless change in the business world. Covered areas: Accounting; Agribusiness Management and Policy; Business Law; Economics and Development Policy; Entrepreneurship and Family Business; Finance; Global Business; Human Resource Management; Information and Communications Technology (ICT); Labor Relations; Marketing; Management Information Systems (MIS); Non-Profit Management; Operations and Supply Chain Management; Organizational Behavior and Theory; Organizational Development; Service Management; Small Business Management; Social Responsibility and Ethics; Strategic Management Policy; Technology and Innovation Management; Tourism and Hospitality Management; Transportation and Logistics