Journal
MICROCHIMICA ACTA
Volume 185, Issue 1, Pages -Publisher
SPRINGER WIEN
DOI: 10.1007/s00604-017-2550-3
Keywords
SELEX; Serum; Fluorescent assay; Limit of detection; Secretory protein; Quenching
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Funding
- Mashhad University of Medical Sciences
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The Mycobacterium Ag85 complex is the major secretory protein of M. tuberculosis. It is a potential marker for early diagnosis of tuberculosis (TB). The authors have identified specific aptamers for Ag85A (FbpA) via protein SELEX using magnetic beads. After twelve rounds of selection, two aptamers (Apt8 and Apt22) were chosen from different groups, and their binding constants were determined by flow cytometry. Apt22 (labeled with Atto 647N) binds to FbpA with high affinity (K-d = 63 nM) and specificity. A rapid, sensitive, and low-cost fluorescent assay was designed based on the use of Apt22 and graphene oxide, with a limit of detection of 1.5 nM and an analytical range from 5 to 200 nM of FbpA.
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