Abstract
Original language | English |
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Article number | 112872 |
Journal | Biosensors and Bioelectronics |
Volume | 175 |
Early online date | 29 Nov 2020 |
DOIs | |
Publication status | Published - 1 Mar 2021 |
Funding
Although the immobilization of the aptamers, with the corresponding conformational constrains, leads to a reduction in their affinity towards the protein, the magnitude of this effect is different in both cases. While the affinity of anti-PSA diminished by two-fold, that of PSAG-1 decreased by more than 100 times. There are two potentially significant differences. First, both aptamers recognize different epitopes on the protein, with different accessibility. Second, the hPSA standard used for titration may contain different glycosylation forms, and it has been previously found that about 77% of the standard PSA isolated from seminal fluid carries core-fucosylated N-glycans (Llop et al., 2016). Nevertheless, the obtained affinities support PSA measurements across the clinical range.We thank Dr. E. Fern?ndez-Rodr?guez and Dr. S. Garc?a-Alonso (Hospital Universitario de Cabue?es-Asturias) for providing the serum samples. The work was funded by the Spanish Ministerio de Ciencia y Universidades (RTI-2018-095756-B-I00), and Principado de Asturias Government (IDI2018-000217), co-financed by FEDER funds. A.D.F. was supported by Asociaci?n Espa?ola contra el C?ncer (AECC) with a Ph.D. fellowship and by Banco Santander and University of Oviedo with a grant in the framework of the economic mobility of excellence grants for teachers and researchers.
Keywords
- Aptasensor
- Glycosylation pattern
- Impedimetric sensor
- Prostate cancer
- PSA
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