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Thiol compounds inhibit the formation of amyloid fibrils by beta 2-microglobulin at neutral pH

Kaori Yamamoto1, Hisashi Yagi, Daisaku Ozawa

  • 1Institute for Protein Research, Osaka University, and CREST, Japan Science and Technology Agency, Yamadaoka 3-2, Suita, Osaka 565-0871, Japan.

Journal of Molecular Biology
|December 25, 2007
PubMed

Insights

Reductants like dithiothreitol and cysteine can prevent beta(2)-microglobulin (beta2-m) amyloid fibril formation. This finding offers a potential strategy to inhibit dialysis-related amyloidosis in patients undergoing long-term hemodialysis.

Area of Science:

  • Biochemistry
  • Medical Science
  • Protein Chemistry

Background:

  • Dialysis-related amyloidosis is common in long-term hemodialysis patients.
  • Beta(2)-microglobulin (beta2-m) is the primary component of amyloid fibrils in this condition.
  • Beta(2)-m's disulfide bond stabilizes its native structure and amyloid fibrils.

Purpose of the Study:

  • To investigate the effect of reductants on beta(2)-m amyloid fibril formation.
  • To explore potential preventative strategies for dialysis-related amyloidosis.

Main Methods:

  • Examined the impact of dithiothreitol and cysteine on beta(2)-m fibrillation at neutral pH.
  • Utilized seed-dependent, ultrasonication-induced, and salt-and-heat-induced fibrillation methods.
  • Assessed fibril formation using Thioflavin T fluorescence, electron microscopy, and circular dichroism.

Main Results:

  • Reductants significantly inhibited seed-dependent and ultrasonication-induced beta(2)-m fibrillation.
  • Amyloid fibril formation was markedly reduced in salt-and-heat-induced fibrillation with reductants.
  • A small number of fibrils still formed even after disulfide bond reduction in agitated conditions.

Conclusions:

  • Reductants like cysteine and dithiothreitol show promise in preventing beta(2)-m amyloid fibril formation.
  • These reductants could be beneficial for inhibiting dialysis-related amyloidosis under physiological conditions.

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