In Vivo and in Vitro Monitoring of Amyloid Aggregation via BSA@FGQDs Multimodal Probe

Yousaf, M, Ahmad, M, Bhatti, I, Nasir, A, Hasan, M, Jian, X, Kalantar-Zadeh, K and Mahmood, N 2019, 'In Vivo and in Vitro Monitoring of Amyloid Aggregation via BSA@FGQDs Multimodal Probe', ACS Sensors, vol. 4, no. 1, pp. 200-210.


Document type: Journal Article
Collection: Journal Articles

Title In Vivo and in Vitro Monitoring of Amyloid Aggregation via BSA@FGQDs Multimodal Probe
Author(s) Yousaf, M
Ahmad, M
Bhatti, I
Nasir, A
Hasan, M
Jian, X
Kalantar-Zadeh, K
Mahmood, N
Year 2019
Journal name ACS Sensors
Volume number 4
Issue number 1
Start page 200
End page 210
Total pages 11
Publisher American Chemical Society
Abstract Early detection of peptide aggregate intermediates is quite challenging because of their variable and complex nature as well as due to lack of reliable sensors for diagnosis. Herein, we report the detection of monomers and oligomers using specified fluorescence and a magnetic resonance imaging (MRI) multimodal probe based on bovine-serum-albumin-capped fluorine functionalized graphene quantum dots (BSA@FGQDs). This probe enables in vitro fluorescence-based monitoring of human islet amyloid polypeptide (hIAPP), insulin, and amyloid β (1-42) (Aβ 42 ) monomers and oligomers during the fibrillogenesis dynamic. Up to 90% fluorescence quenching of BSA@FGQDs probe upon addition of amyloid monomers/oligomers was observed due to static quenching and nonradiative energy transfer. Moreover, the BSA@FGQDs probe shows 10 times higher signals in detecting amyloid intermediates and fibrils than that of conventional thioflavin dye. A negative Î"G° value (-36.21 kJ/mol) indicates spontaneous interaction of probe with the peptide. These interactions are hydrogen bonding and hydrophobic as proved by thermodynamic parameters. Visual binding clues of BSA@FGQDs with different morphological states of amyloid protein was achieved through electron microscopy. Furthermore, intravenous and intracranial injection of BSA@FGQDs probe in Alzheimer model mice brain enabled in vivo detection of amyloid plaques in live mice brain by 19 F MRI through contrast enhancement. Our proposed probe not only effectively monitors in vitro fibrillation kinetics of number of amyloid proteins with higher sensitivity and specificity than thioflavin dye, but also, the presence of a 19 F center makes BSA@FGQDs an effective probe as a noninvasive and nonradiative in vivo detection probe for amyloid plaques.
Subject Nanophotonics
Industrial Biotechnology Diagnostics (incl. Biosensors)
Chemical Engineering Design
Keyword(s) 19F magnetic resonance imaging
amyloid fibrillation monitoring
contrast agent
fluorographene quantum dots
multimodal probe
DOI - identifier 10.1021/acssensors.8b01216
Copyright notice © 2018 American Chemical Society
ISSN 2379-3694
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 2 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 0 times in Scopus Article
Altmetric details:
Access Statistics: 5 Abstract Views  -  Detailed Statistics
Created: Mon, 29 Apr 2019, 13:04:00 EST by Catalyst Administrator
© 2014 RMIT Research Repository • Powered by Fez SoftwareContact us