RT Journal Article
T1 Towards Ratiometric Sensing of Amyloid Fibrils In Vitro
A1 Freire Rodríguez, Sonia
A1 Rodríguez-Prieto, Flor
A1 Ríos Rodríguez, María del Carmen
A1 Penedo Esteiro, Juan Carlos
A1 Al-Soufi, Wajih
A1 Novo, Mercedes
K1 Amyloid‐beta peptides
K1 Charge transfer
K1 Fluorescent probes
K1 Photophysics
K1 Proton transfer
AB The aggregation of amyloid‐β peptide and its accumulation in the human brain has an important role in the etiology of Alzheimer’s disease. Thioflavin T has been widely used as a fluorescent marker for these amyloid aggregates. Nevertheless, its complex photophysical behavior, with strong wavelength dependencies of all its fluorescence properties, requires searching for new fluorescent probes. The use of 2‐(2′‐hydroxyphenyl)imidazo[4,5‐b]pyridine (HPIP), which shows two emission bands and a rich excited‐state behavior due to the existence of excited‐state intramolecular processes of proton transfer and charge transfer, is proposed. These properties result in a high sensitivity of HPIP fluorescence to its microenvironment and cause a large differential fluorescence enhancement of the two bands upon binding to aggregates of the amyloid‐β peptide. Based on this behavior, a very sensitive ratiometric method is established for the detection and quantification of amyloid fibrils, which can be combined with the monitoring of fluorescence anisotropy. The binding selectivity of HPIP is discussed on the basis of the apparent binding equilibrium constants of this probe to amyloid‐β (1–42) fibrils and to the nonfibrillar protein bovine serum albumin. Finally, an exhaustive comparison between HPIP and thioflavin T is presented to discuss the sensitivity and specificity of these probes to amyloid aggregates and the significant advantages of the HPIP dye for quantitative determinations
PB Wiley
YR 2015
FD 2015
LK http://hdl.handle.net/10347/17053
UL http://hdl.handle.net/10347/17053
LA eng
NO Freire, S. , Rodríguez‐Prieto, F. , Ríos Rodríguez, M. C., Penedo, J. C., Al‐Soufi, W. and Novo, M. (2015), Towards Ratiometric Sensing of Amyloid Fibrils In Vitro. Chem. Eur. J., 21: 3425-3434. doi:10.1002/chem.201406110
NO This is the peer-reviewed version of the following article: Chemistry - A European Journal 2015, 21, 3425–3434, DOI: 10.1002/chem.201406110. The final form has been published at https://onlinelibrary.wiley.com/doi/abs/10.1002/chem.201406110.This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions
NO Xunta de GaliciaEuropean Regional Development FundMinisterio de Ciencia e InnovaciónXunta de Galicia. Grant Numbers: CTQ2010‐21369, CTQ2010‐17835, GPC2013/052, R2014/051RS MacDonald Charitable Trust
DS Minerva
RD 22 abr 2026