A computational study on how structure influences the optical properties in model crystal structures of amyloid fibrils. Issue 5 (23rd January 2017)

• Record Type: Journal Article
• Authors: Grisanti, Luca; Pinotsi, Dorothea; Gebauer, Ralph; Kaminski Schierle, Gabriele S.; Hassanali, Ali A.
• Is Part Of: Physical chemistry chemical physics. Volume 19:Issue 5(2017)
• Page Start: 4030
• Page End: 4040
• Publication Date: 2017-01-23
• Subjects: Chemistry, Physical and theoretical -- Periodicals; 541.3
• DOI: 10.1039/c6cp07564a
• Languages: English
• ISSNs: 1463-9076

Abstract

Abstract : Different types of hydrogen bonding interactions that occur in amyloids model systems and molecular factors that control the susceptibility of the protons to undergo proton transfer and how this couples to the optical properties. Abstract : Amyloid fibrils have been shown to have peculiar optical properties since they can exhibit fluorescence in the absence of aromatic residues. In a recent study, we have shown that proton transfer (PT) events along hydrogen bonds (HBs) are coupled to absorption in the near UV range. Here, we gain more insights into the different types of hydrogen bonding interactions that occur in our model systems and the molecular factors that control the susceptibility of the protons to undergo PT and how this couples to the optical properties. In the case of the strong N–C termini interactions, a nearby methionine residue stabilizes the non-zwitterionic NH2 –COOH pair, while zwitterionic NH3 + –COO– is stabilized by the proximity of nearby crystallographic water molecules. Proton motion along the hydrogen bonds in the fibril is intimately coupled to the compression of the heavier atoms, similar to what is observed in bulk water. Small changes in the compression of the hydrogen bonds in the protein can lead to significant changes in both the ground and excited state potential energy surfaces associated with PT. Finally, we also reinforce the importance of nuclear quantum fluctuations of protons in the HBs of the amyloid proteins.