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Updated: Aug 16, 2026

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
06:27

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

Molecular interactions in the formation and deposition of beta2-microglobulin-related amyloid fibrils

Hironobu Naiki1, Suguru Yamamoto, Kazuhiro Hasegawa

  • 1Division of Molecular Pathology, Department of Pathological Sciences, Faculty of Medical Sciences, University of Fukui, Fukui, Japan. naiki@fmsrsa.fukui-med.ac.jp

Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis
|August 4, 2005
PubMed

Insights

Beta2-microglobulin amyloidosis involves beta2-microglobulin (beta2-m) unfolding. Amyloid-associated molecules like apoE, GAGs, and PGs influence beta2-m fibril formation and stability.

Area of Science:

  • Biochemistry
  • Medical Science
  • Protein Chemistry

Background:

  • Beta2-microglobulin (beta2-m) amyloidosis is a complication for dialysis patients.
  • Partial unfolding of beta2-m is a prerequisite for amyloid fibril formation.
  • Amyloid-associated molecules (apoE, GAGs, PGs) may play a role in A beta2M amyloidosis.

Purpose of the Study:

  • To investigate the role of amyloid-associated molecules in beta2-microglobulin (beta2-m) amyloid fibril formation and stability.
  • To understand the mechanisms by which molecules like TFE, SDS, apoE, GAGs, and PGs influence beta2-m amyloidogenesis at neutral pH.

Main Methods:

  • In vitro studies of beta2-microglobulin (beta2-m) fibril formation.
  • Utilizing agents like 2,2,2-trifluoroethanol (TFE) and sodium dodecyl sulfate (SDS) at neutral pH.
  • Assessing the effects of apolipoprotein E (apoE), glycosaminoglycans (GAGs), and proteoglycans (PGs) on beta2-m fibril stability and extension.

Main Results:

  • Low concentrations of TFE and SDS induce beta2-m fibril extension and stabilization at neutral pH.
  • ApoE, GAGs, and PGs form stable complexes with beta2-m amyloid fibrils, enhancing stability at neutral pH.
  • Heparin and biglycan show specific enhancing effects on fibril extension and polymerization, respectively.

Conclusions:

  • Specific molecules significantly impact beta2-m conformation and amyloid fibril stability.
  • These molecular interactions are crucial for the deposition of A beta2M amyloid fibrils in vivo.
  • Findings support the hypothesis that amyloid-associated molecules modulate beta2-m amyloidosis progression.

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