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Abstract
We combine absorption and fluorscence spectroscopy experiments and theoretical modeling to specifically examine the role of termini interactions on the optical properties.
Optical absorption and fluorescence is measured for a six-chain amino acid 2Y3J (AIIGLM) which forms a segment of the full amyloid beta 1-40. In order to explore the sensitivity of the optical properties to the termini interactions, the experiments were repeated by acetylating the N-terminus.
Although atomic force microscopy experiments indicate the formation of some form of fibrilar or crystal aggregates in both systems, the optical properties are strikingly different - acetylation significantly reduces optical activity between 280-350 nm.
Supplementary materials
Title
chemrxiv optical amyloid si
Description
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