{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Xu H"],"funding":["NIGMS NIH HHS"],"pagination":["89-96"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3566859"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9"],"pubmed_abstract":["The fluorophosphonate (FP) moiety attached to a biotin tag is a prototype chemical probe used to quantitatively analyze and enrich active serine hydrolases in complex proteomes in an approach called activity-based protein profiling (ABPP). In this study we have designed a novel synthetic route to a known FP probe linked by polyethylene glycol to a biotin tag (FP-PEG-biotin). Our route markedly increases the efficiency of the probe synthesis and overcomes several problems of a prior synthesis. As a proof of principle, FP-PEG-biotin was evaluated against isolated protein mixtures and different rat-tissue homogenates, showing its ability to specifically target serine hydrolases. We also assessed the ability of FP-PEG-biotin to compete with substrates that have high enzyme turnover rates. The "],"journal":["Beilstein journal of organic chemistry"],"pubmed_title":["An improved synthesis of a fluorophosphonate-polyethylene glycol-biotin probe and its use against competitive substrates."],"pmcid":["PMC3566859"],"funding_grant_id":["R01 GM037188"],"pubmed_authors":["Sabit H","Showalter HDH","Xu H","Amidon GL"],"additional_accession":[]},"is_claimable":false,"name":"An improved synthesis of a fluorophosphonate-polyethylene glycol-biotin probe and its use against competitive substrates.","description":"The fluorophosphonate (FP) moiety attached to a biotin tag is a prototype chemical probe used to quantitatively analyze and enrich active serine hydrolases in complex proteomes in an approach called activity-based protein profiling (ABPP). In this study we have designed a novel synthetic route to a known FP probe linked by polyethylene glycol to a biotin tag (FP-PEG-biotin). Our route markedly increases the efficiency of the probe synthesis and overcomes several problems of a prior synthesis. As a proof of principle, FP-PEG-biotin was evaluated against isolated protein mixtures and different rat-tissue homogenates, showing its ability to specifically target serine hydrolases. We also assessed the ability of FP-PEG-biotin to compete with substrates that have high enzyme turnover rates. The ","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013","modification":"2025-04-04T10:12:00.386Z","creation":"2019-03-27T01:04:29Z"},"accession":"S-EPMC3566859","cross_references":{"pubmed":["23400700"],"doi":["10.3762/bjoc.9.12"]}}