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Low Energy Optical Excitations as an Indicator of Structural Changes Initiated at the Termini of Amyloid Protein

Abstract

There is a growing body of experimental work showing that protein aggregates associated with amyloid fibrils feature an intrinsic fluorescence. In order to understand the microscopic origin of this behavior observed in non-aromatic aggregates of peptides and proteins, we conducted a combined experimental and computational study on the optical properties of amyloid-derived oligopeptides in the near-UV region. We have focused on a few model systems having charged termini (zwitterionic) or acetylated termini. For the zwitterionic system, we were able to simulate the longer tail absorption in the near UV (250-350 nm), supporting the experimental results in term of excitation spectra. We analyzed optical excitations responsible for the low-energy absorption and found a large role played by charge-transfer states around the termini. These charge-transfer excitations are very sensitive to the conformation of the peptide and in the realistic fibrils may involve inter and intra chain charge reorganization.

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Publication details

The article was received on 22 Aug 2019, accepted on 04 Oct 2019 and first published on 07 Oct 2019


Article type: Paper
DOI: 10.1039/C9CP04648H
Phys. Chem. Chem. Phys., 2019, Accepted Manuscript

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    Low Energy Optical Excitations as an Indicator of Structural Changes Initiated at the Termini of Amyloid Protein

    K. Jong, Y. Taghipour Azar, L. Grisanti, A. D. Stephens, S. T. E. Jones, D. Credgington, G. S. Kaminski Schierle and A. A. Hassanali, Phys. Chem. Chem. Phys., 2019, Accepted Manuscript , DOI: 10.1039/C9CP04648H

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