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Cyclophilin B function elucidated by electrochemical sensors

ABSTRACT: We have investigated the function of CypB through negative ionization high resolution LCMS and examined the purity of a CypB protein with intact mass analyzes on a Q Exactive mass spectrometer.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Benjamin C Orsburn

PROVIDER: MSV000089498 | MassIVE | Thu May 19 17:00:00 BST 2022

REPOSITORIES: MassIVE

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Publications

Human Cyclophilin B Nuclease Activity Revealed via Nucleic Acid-Based Electrochemical Sensors.

Clark Vincent V Waters Kelly K Orsburn Ben B Bumpus Namandjé N NN Kundu Nandini N Sczepanski Jonathan T JT Ray Partha P Arroyo-Currás Netzahualcóyotl N

Angewandte Chemie (International ed. in English) 20221006 45

Human cyclophilin B (CypB) is oversecreted by pancreatic cancer cells, making it a potential biomarker for early-stage disease diagnosis. Our group is motivated to develop aptamer-based assays to measure CypB levels in biofluids. However, human cyclophilins have been postulated to have collateral nuclease activity, which could impede the use of aptamers for CypB detection. To establish if CypB can hydrolyze electrode-bound nucleic acids, we used ultrasensitive electrochemical sensors to measure ...[more]

PMID: 35999181

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