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- Title
Chirality and Chiroptical Properties of Amyloid Fibrils.
- Authors
Dzwolak, Wojciech
- Abstract
ABSTRACT Chirality of amyloid fibrils-linear beta-sheet-rich aggregates of misfolded protein chains-often manifests in morphological traits such as helical twist visible in and in chiroptical properties accessible to vibrational circular dichroism (VCD). According to recent studies the relationship between molecular chirality of polypeptide and superstructural chirality of amyloid fibrils may be more intricate and less deterministic than previously assumed. Several puzzling experimental findings have put into question earlier intuitive ideas on: 1) the bottom-up chirality transfer upon amyloidogenic self-assembly, and 2) the structural origins of chiroptical properties of protein aggregates. For example, removal of a single amino acid residue from an amyloidogenic all-L peptide was shown to reverse handedness of fibrils. On the other hand, certain types of amyloid aggregates revealed surprisingly strong VCD spectra with the sign and shape dependent on the conditions of fibrillation. Hence, microscopic and chiroptical studies have highlighted chirality as one more aspect of polymorphism of amyloid fibrils. This brief review is intended to outline the current state of research on amyloid-like fibrils from the perspective of their structural and superstructural chirality and chiroptical properties. Chirality 26:220-227, 2014. © 2014 Wiley Periodicals, Inc.
- Subjects
AMYLOID beta-protein; CHIRALITY; PROTEIN folding; CIRCULAR dichroism; AMINO acid residues; OPTICAL properties measurement
- Publication
Chirality, 2014, Vol 26, Issue 9, p220
- ISSN
0899-0042
- Publication type
Article
- DOI
10.1002/chir.22335