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10.1371/journal.pone.0153360 http://scihub22266oqcxt.onion/10.1371/journal.pone.0153360 C4838334!4838334!27096746     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27096746&cmd=llinks): Failed to open stream: HTTP request failed! 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Design of Peptide Substrate for Sensitively and Specifically Detecting Two A?-Degrading Enzymes: Neprilysin and Angiotensin-Converting Enzyme |pdf=|usr=}}{{27096746}} gab.com Text Design of Peptide Substrate for Sensitively and Specifically Detecting Two A -Degrading Enzymes: Neprilysin and Angiotensin-Converting Enzyme JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=27096746 #FOAvip Upregulation of neprilysin (NEP) to reduce A? accumulation in the brain is a promising strategy for the prevention of Alzheimer?s disease (AD). This report describes the design and synthesis of a quenched fluorogenic peptide substrate qf-A?(12?16)AAC (with the sequence VHHQKAAC), which has a fluorophore, Alexa-350, linked to the side-chain of its C-terminal cysteine and a quencher, Dabcyl, linked to its N-terminus. This peptide emitted strong fluorescence upon cleavage. Our results showed that qf-A?(12?16)AAC is more sensitive to NEP than the previously reported peptide substrates, so that concentrations of NEP as low as 0.03 nM could be detected at peptide concentration of 2 ?M. Moreover, qf-A?(12?16)AAC had superior enzymatic specificity for both NEP and angiotensin-converting enzyme (ACE), but was inert with other A?-degrading enzymes. This peptide, used in conjunction with a previously reported peptide substrate qf-A?(1?7)C [which is sensitive to NEP and insulin-degrading enzyme (IDE)], could be used for high-throughput screening of compounds that only upregulate NEP. The experimental results of cell-based activity assays using both qf-A?(1?7)C and qf-A?(12?16)AAC as the substrates confirm that somatostatin treatment most likely upregulates IDE, but not NEP, in neuroblastoma cells. Twit Text FOAVip Design of Peptide Substrate for Sensitively and Specifically Detecting Two A -Degrading Enzymes: Neprilysin and Angiotensin-Converting Enzyme ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=27096746 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27096746 #FOAvip English Wikipedia <ref>{{Cite pmid|27096746}}</ref> Design of Peptide Substrate for Sensitively and Specifically Detecting Two A?-Degrading Enzymes: Neprilysin and Angiotensin-Converting Enzyme #MMPMID27096746 Chen PT; Chen CL; Lin LTW; Lo CH; Hu CJ; Chen RPY; Wang SSS PLoS One 2016[]; 11 (4): ä PMID27096746show ga Upregulation of neprilysin (NEP) to reduce A? accumulation in the brain is a promising strategy for the prevention of Alzheimer?s disease (AD). This report describes the design and synthesis of a quenched fluorogenic peptide substrate qf-A?(12?16)AAC (with the sequence VHHQKAAC), which has a fluorophore, Alexa-350, linked to the side-chain of its C-terminal cysteine and a quencher, Dabcyl, linked to its N-terminus. This peptide emitted strong fluorescence upon cleavage. Our results showed that qf-A?(12?16)AAC is more sensitive to NEP than the previously reported peptide substrates, so that concentrations of NEP as low as 0.03 nM could be detected at peptide concentration of 2 ?M. Moreover, qf-A?(12?16)AAC had superior enzymatic specificity for both NEP and angiotensin-converting enzyme (ACE), but was inert with other A?-degrading enzymes. This peptide, used in conjunction with a previously reported peptide substrate qf-A?(1?7)C [which is sensitive to NEP and insulin-degrading enzyme (IDE)], could be used for high-throughput screening of compounds that only upregulate NEP. The experimental results of cell-based activity assays using both qf-A?(1?7)C and qf-A?(12?16)AAC as the substrates confirm that somatostatin treatment most likely upregulates IDE, but not NEP, in neuroblastoma cells. äDesign of Peptide Substrate for Sensitively and Specifically Detecting(epmc).pdf DeepDyve Pubget Overpricing