| Autor: |
Safar W; IMMM - UMR 6283 CNRS, Le Mans Université, Avenue Olivier Messiaen, 72085 Le Mans, Cedex 9, France. marc.lamydelachapelle@univ-lemans.fr., Tatar AS, Leray A, Potara M, Liu Q, Edely M, Djaker N, Spadavecchia J, Fu W, Derouich SG, Felidj N, Astilean S, Finot E, Lamy de la Chapelle M |
| Jazyk: |
angličtina |
| Zdroj: |
Nanoscale [Nanoscale] 2021 Aug 07; Vol. 13 (29), pp. 12443-12453. Date of Electronic Publication: 2021 Jul 12. |
| DOI: |
10.1039/d1nr02180j |
| Abstrakt: |
We study the interaction between one aptamer and its analyte (the MnSOD protein) by the combination of surface-enhanced Raman scattering and multivariate statistical analysis. We observe the aptamer structure and its evolution during the interaction under different experimental conditions (in air or in buffer). Through the spectral treatment by principal component analysis of a large set of SERS data, we were able to probe the aptamer conformations and orientations relative to the surface assuming that the in-plane nucleoside modes are selectively enhanced. We demonstrate that the aptamer orientation and thus its flexibility rely strongly on the presence of a spacer of 15 thymines and on the experimental conditions with the aptamer lying on the surface in air and standing in the buffer. We reveal for the first time that the interaction with MnSOD induces a large loss of flexibility and freezes the aptamer structure in a single conformation. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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