Further characterization of the target of a potential aptamer biomarker for pancreatic cancer: cyclophilin B and its posttranslational modifications.

Published

Journal Article

Posttranslational modifications on proteins can serve as useful biomarkers for disease. However, their discovery and detection in biological fluids is challenging. Aptamers are oligonucleotide ligands that demonstrate high affinity toward their target proteins and can discriminate closely related proteins with superb specificity. Previously, we generated a cyclophilin B aptamer (M9-5) that could discriminate sera from pancreatic cancer patients and healthy volunteers with high specificity and sensitivity. In our present work we further characterize the aptamer and the target protein, cyclophilin B, and demonstrate that the aptamer could discriminate between cyclophilin B expressed in human cells versus bacteria. Using mass-spectrometric analysis, we discovered post-translational modifications on cyclophilin B that might be responsible for the M9-5 selectivity. The ability to distinguish between forms of the same protein with differing post-translational modifications is an important advantage of aptamers as tools for identification and detection of biomarkers.

Full Text

Duke Authors

Cited Authors

  • Ray, P; Sullenger, BA; White, RR

Published Date

  • December 2013

Published In

Volume / Issue

  • 23 / 6

Start / End Page

  • 435 - 442

PubMed ID

  • 24152208

Pubmed Central ID

  • 24152208

Electronic International Standard Serial Number (EISSN)

  • 2159-3345

Digital Object Identifier (DOI)

  • 10.1089/nat.2013.0439

Language

  • eng

Conference Location

  • United States