Chirality‐Assisted Ring‐Like Aggregation of Aβ(1–40) at Liquid–Solid Interfaces: A Stereoselective Two‐Step Assembly Process
- 22 December 2014
- journal article
- research article
- Published by Wiley in Angewandte Chemie
- Vol. 54 (7), 2245-2250
- https://doi.org/10.1002/anie.201410768
Abstract
Molecular chirality is introduced at liquid–solid interfaces. A ring-like aggregation of amyloid Aβ(1–40) on N-isobutyryl-L-cysteine (L-NIBC)-modified gold substrate occurs at low Aβ(1–40) concentration, while D-NIBC modification only results in rod-like aggregation. Utilizing atomic force microscope controlled tip-enhanced Raman scattering, we directly observe the secondary structure information for Aβ(1–40) assembly in situ at the nanoscale. D- or L-NIBC on the surface can guide parallel or nonparallel alignment of β-hairpins through a two-step process based on electrostatic-interaction-enhanced adsorption and subsequent stereoselective recognition. Possible electrostatic interaction sites (R5 and K16) and a chiral recognition site (H14) of Aβ(1–40) are proposed, which may provide insight into the understanding of this effect.Funding Information
- National Natural Science Foundation of China (91127027, 51173142, 21105078)
- China National Funds for Distinguished Young Scientists (51325302)
- Major State Basic Research Development Program of China (2013CB933002)
- Program for Changjiang Scholars and Innovative Research Team in University (IRT1169)
- Program of Introducing Talents of Discipline to Universities (B13035)
This publication has 73 references indexed in Scilit:
- Molecular Structures of Amyloid and Prion Fibrils: Consensus versus ControversyAccounts of Chemical Research, 2013
- Role of β-Hairpin Formation in Aggregation: The Self-Assembly of the Amyloid-β(25–35) PeptideBiophysical Journal, 2012
- A Diversity of Assembly Mechanisms of a Generic Amyloid FoldMolecular Cell, 2011
- 3D structure of Alzheimer's amyloid-β(1–42) fibrilsProceedings of the National Academy of Sciences of the United States of America, 2005
- Exploring the Early Steps of Amyloid Peptide Aggregation by ComputersAccounts of Chemical Research, 2005
- Evidence of the Existence of Micelles in the Fibrillogenesis of β-Amyloid PeptideThe Journal of Physical Chemistry B, 2005
- Natural oligomers of the amyloid-β protein specifically disrupt cognitive functionNature Neuroscience, 2004
- Protein folding and misfoldingNature, 2003
- The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to TherapeuticsScience, 2002
- Amyloid β-peptide is produced by cultured cells during normal metabolismNature, 1992