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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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Amyloid Fibrils03:03

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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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Chirality-assisted ring-like aggregation of aβ(1-40) at liquid-solid interfaces: a stereoselective two-step assembly

Guanbin Gao1, Mingxi Zhang, Pei Lu

  • 1State Key Laboratory of Advanced Technology for Materials Synthesis and Processing, Wuhan University of Technology, Wuhan 430070 (PR China).

Angewandte Chemie (International Ed. in English)
|December 24, 2014
PubMed
Summary

Chiral surfaces of N-isobutyryl-L-cysteine (L-NIBC) and D-NIBC influence amyloid beta Aβ(1-40) assembly, forming distinct ring-like or rod-like structures. This study reveals nanoscale control over protein aggregation using chiral interfaces.

Keywords:
amyloidschiralitystereoselectivitysurface assemblysurface interactions

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Area of Science:

  • Surface Chemistry
  • Biophysics
  • Nanotechnology

Background:

  • Molecular chirality plays a crucial role in biological systems.
  • Amyloid proteins, such as Aβ(1-40), are implicated in various diseases.
  • Controlling protein aggregation at interfaces is vital for understanding biological processes and developing new materials.

Purpose of the Study:

  • To investigate the influence of chiral surfaces on the assembly of amyloid Aβ(1-40).
  • To observe and characterize the nanoscale secondary structure of Aβ(1-40) aggregates in situ.
  • To elucidate the mechanisms underlying chiral recognition and guided protein assembly.

Main Methods:

  • Modification of gold substrates with N-isobutyryl-L-cysteine (L-NIBC) and its enantiomer D-NIBC.
  • Atomic force microscopy (AFM) for high-resolution imaging of protein aggregates.
  • Tip-enhanced Raman scattering (TERS) for nanoscale secondary structure analysis of Aβ(1-40) assembly.

Main Results:

  • Low concentrations of Aβ(1-40) formed ring-like aggregates on L-NIBC modified surfaces.
  • D-NIBC modified surfaces resulted in rod-like aggregation of Aβ(1-40).
  • AFM-TERS directly visualized nanoscale secondary structures and guided alignment of β-hairpins in Aβ(1-40) assemblies.

Conclusions:

  • Chiral surfaces can effectively control the morphology and alignment of amyloid Aβ(1-40) aggregates.
  • A two-step process involving electrostatic interactions and stereoselective recognition dictates the assembly.
  • Proposed interaction sites (R5, K16, H14) on Aβ(1-40) offer insights into chiral recognition mechanisms at liquid-solid interfaces.