Human Cyclophilin B Nuclease Activity Revealed via Nucleic Acid‐Based Electrochemical Sensors
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 nu...
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| Published in | Angewandte Chemie International Edition Vol. 61; no. 45; pp. e202211292 - n/a |
|---|---|
| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Germany
Wiley Subscription Services, Inc
07.11.2022
John Wiley and Sons Inc |
| Edition | International ed. in English |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1433-7851 1521-3773 1521-3773 |
| DOI | 10.1002/anie.202211292 |
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| Abstract | 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 CypB's hydrolytic activity. Our sensors use ssDNA and dsDNA in the biologically predominant d‐DNA form, and in the nuclease resistant l‐DNA form. Challenging such sensors with CypB and control proteins, we unequivocally demonstrate that CypB can cleave nucleic acids. To our knowledge, this is the first study to use electrochemical biosensors to reveal the hydrolytic activity of a protein that is not known to be a nuclease. Future development of CypB bioassays will require the use of nuclease‐resistant aptamer sequences.
This study employs electrochemical DNA‐based sensors to investigate the hydrolytic activity of a previously unknown nuclease, cyclophilin B. The protein is secreted by pancreatic cancer cells and could be a biomarker for early‐stage cancer diagnoses. However, the demonstrated nuclease activity will limit bioassay development based on natural nucleic acid aptamers. Instead, we propose DNA stereoisomers (l‐DNA) to overcome this challenge. |
|---|---|
| AbstractList | 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 CypB's hydrolytic activity. Our sensors use ssDNA and dsDNA in the biologically predominant
d
‐DNA form, and in the nuclease resistant
l
‐DNA form. Challenging such sensors with CypB and control proteins, we unequivocally demonstrate that CypB can cleave nucleic acids. To our knowledge, this is the first study to use electrochemical biosensors to reveal the hydrolytic activity of a protein that is not known to be a nuclease. Future development of CypB bioassays will require the use of nuclease‐resistant aptamer sequences.
This study employs electrochemical DNA‐based sensors to investigate the hydrolytic activity of a previously unknown nuclease, cyclophilin B. The protein is secreted by pancreatic cancer cells and could be a biomarker for early‐stage cancer diagnoses. However, the demonstrated nuclease activity will limit bioassay development based on natural nucleic acid aptamers. Instead, we propose DNA stereoisomers (
l
‐DNA) to overcome this challenge. 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 CypB's hydrolytic activity. Our sensors use ssDNA and dsDNA in the biologically predominant d-DNA form, and in the nuclease resistant l-DNA form. Challenging such sensors with CypB and control proteins, we unequivocally demonstrate that CypB can cleave nucleic acids. To our knowledge, this is the first study to use electrochemical biosensors to reveal the hydrolytic activity of a protein that is not known to be a nuclease. Future development of CypB bioassays will require the use of nuclease-resistant aptamer sequences.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 CypB's hydrolytic activity. Our sensors use ssDNA and dsDNA in the biologically predominant d-DNA form, and in the nuclease resistant l-DNA form. Challenging such sensors with CypB and control proteins, we unequivocally demonstrate that CypB can cleave nucleic acids. To our knowledge, this is the first study to use electrochemical biosensors to reveal the hydrolytic activity of a protein that is not known to be a nuclease. Future development of CypB bioassays will require the use of nuclease-resistant aptamer sequences. 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 CypB's hydrolytic activity. Our sensors use ssDNA and dsDNA in the biologically predominant d ‐DNA form, and in the nuclease resistant l ‐DNA form. Challenging such sensors with CypB and control proteins, we unequivocally demonstrate that CypB can cleave nucleic acids. To our knowledge, this is the first study to use electrochemical biosensors to reveal the hydrolytic activity of a protein that is not known to be a nuclease. Future development of CypB bioassays will require the use of nuclease‐resistant aptamer sequences. 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 CypB's hydrolytic activity. Our sensors use ssDNA and dsDNA in the biologically predominant d‐DNA form, and in the nuclease resistant l‐DNA form. Challenging such sensors with CypB and control proteins, we unequivocally demonstrate that CypB can cleave nucleic acids. To our knowledge, this is the first study to use electrochemical biosensors to reveal the hydrolytic activity of a protein that is not known to be a nuclease. Future development of CypB bioassays will require the use of nuclease‐resistant aptamer sequences. 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 CypB's hydrolytic activity. Our sensors use ssDNA and dsDNA in the biologically predominant d‐DNA form, and in the nuclease resistant l‐DNA form. Challenging such sensors with CypB and control proteins, we unequivocally demonstrate that CypB can cleave nucleic acids. To our knowledge, this is the first study to use electrochemical biosensors to reveal the hydrolytic activity of a protein that is not known to be a nuclease. Future development of CypB bioassays will require the use of nuclease‐resistant aptamer sequences. This study employs electrochemical DNA‐based sensors to investigate the hydrolytic activity of a previously unknown nuclease, cyclophilin B. The protein is secreted by pancreatic cancer cells and could be a biomarker for early‐stage cancer diagnoses. However, the demonstrated nuclease activity will limit bioassay development based on natural nucleic acid aptamers. Instead, we propose DNA stereoisomers (l‐DNA) to overcome this challenge. |
| Author | Waters, Kelly Arroyo‐Currás, Netzahualcóyotl Orsburn, Ben Ray, Partha Bumpus, Namandjé N. Sczepanski, Jonathan T. Clark, Vincent Kundu, Nandini |
| AuthorAffiliation | 3 Department of Chemistry Texas A&M University College Station Texas TX 77842 USA 2 Department of Pharmacology and Molecular Sciences Johns Hopkins University School of Medicine Baltimore MD 21205 USA 4 Department of Surgery Division of Surgical Oncology Moores Cancer Center Department of Medicine Division of Infectious Diseases and Global Public Health University of California San Diego Health San Diego CA 92093 USA 1 Chemistry-Biology Interface Program Zanvyl Krieger School of Arts & Sciences Johns Hopkins University Baltimore MD 21218 USA |
| AuthorAffiliation_xml | – name: 4 Department of Surgery Division of Surgical Oncology Moores Cancer Center Department of Medicine Division of Infectious Diseases and Global Public Health University of California San Diego Health San Diego CA 92093 USA – name: 1 Chemistry-Biology Interface Program Zanvyl Krieger School of Arts & Sciences Johns Hopkins University Baltimore MD 21218 USA – name: 3 Department of Chemistry Texas A&M University College Station Texas TX 77842 USA – name: 2 Department of Pharmacology and Molecular Sciences Johns Hopkins University School of Medicine Baltimore MD 21205 USA |
| Author_xml | – sequence: 1 givenname: Vincent surname: Clark fullname: Clark, Vincent organization: Johns Hopkins University – sequence: 2 givenname: Kelly surname: Waters fullname: Waters, Kelly organization: Johns Hopkins University School of Medicine – sequence: 3 givenname: Ben surname: Orsburn fullname: Orsburn, Ben organization: Johns Hopkins University School of Medicine – sequence: 4 givenname: Namandjé N. surname: Bumpus fullname: Bumpus, Namandjé N. organization: Johns Hopkins University School of Medicine – sequence: 5 givenname: Nandini surname: Kundu fullname: Kundu, Nandini organization: Texas A&M University College Station – sequence: 6 givenname: Jonathan T. surname: Sczepanski fullname: Sczepanski, Jonathan T. organization: Texas A&M University College Station – sequence: 7 givenname: Partha surname: Ray fullname: Ray, Partha email: pray@health.ucsd.edu organization: University of California San Diego Health – sequence: 8 givenname: Netzahualcóyotl orcidid: 0000-0002-2740-6276 surname: Arroyo‐Currás fullname: Arroyo‐Currás, Netzahualcóyotl email: netzarroyo@jhmi.edu organization: Johns Hopkins University School of Medicine |
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| CitedBy_id | crossref_primary_10_1016_j_coelec_2023_101286 crossref_primary_10_1021_acs_analchem_2c05158 crossref_primary_10_1021_acsnano_4c11857 crossref_primary_10_1016_j_bioelechem_2024_108651 |
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| Keywords | Biomarker Nuclease Pancreatic Cancer Cyclophilin B Aptamer-Based Sensors |
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| Snippet | Human cyclophilin B (CypB) is oversecreted by pancreatic cancer cells, making it a potential biomarker for early‐stage disease diagnosis. Our group is... Human cyclophilin B (CypB) is oversecreted by pancreatic cancer cells, making it a potential biomarker for early-stage disease diagnosis. Our group is... |
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| SubjectTerms | Aptamer-Based Sensors Aptamers Bioassays Biomarker Biomarkers Biosensors Chemical sensors Cyclophilin B Cyclophilins - metabolism Deoxyribonucleic acid DNA Electrochemical Techniques Electrochemistry Endonucleases Humans Nuclease Nucleic Acids Pancreatic Cancer Pancreatic Neoplasms Peptidylprolyl isomerase Proteins |
| Title | Human Cyclophilin B Nuclease Activity Revealed via Nucleic Acid‐Based Electrochemical Sensors |
| URI | https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fanie.202211292 https://www.ncbi.nlm.nih.gov/pubmed/35999181 https://www.proquest.com/docview/2730420964 https://www.proquest.com/docview/2706182857 https://pubmed.ncbi.nlm.nih.gov/PMC9633453 |
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