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Updated: Apr 2, 2026

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
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pH-Driven Distinct Aggregation Pathways of Human γD-Crystallin.

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  • 1School of Biotechnology, Jawaharlal Nehru University, New Delhi 110067, India.

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|April 1, 2026
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Summary
This summary is machine-generated.

Human γD-Crystallin aggregation pathways differ significantly with pH. Acidic conditions promote amyloid fibril formation, while physiological pH leads to amorphous aggregates, offering insights into cataract mechanisms.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Ophthalmology

Background:

  • Human γD-Crystallin is crucial for eye lens transparency.
  • Protein aggregation, despite its stability, contributes to cataract formation.

Purpose of the Study:

  • To investigate distinct aggregation pathways of human γD-Crystallin.
  • To elucidate the influence of pH and temperature on aggregation.
  • To provide mechanistic insights into γD-Crystallin-related cataracts.

Main Methods:

  • Aggregation studies conducted at varying pH (2.0, 4.5, 7.4) and temperature (65 °C).
  • Techniques included Thioflavin T (ThT) and Nile red fluorescence, transmission electron microscopy (TEM), Fourier transform infrared (FT-IR) spectroscopy, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), matrix-assisted laser desorption ionization-time-of-flight (MALDI-TOF), circular dichroism (CD) spectroscopy, and 8-anilinonaphthalene-1-sulfonic acid (ANS) fluorescence.

Main Results:

  • At pH 2.0 and 65 °C, amyloid fibrils with fragmentation were observed.
  • At pH 4.5 and 65 °C, amyloid fibrils formed without fragmentation, indicating conformational changes.
  • At physiological pH 7.4 and 65 °C, amorphous aggregates formed, lacking cross-β-sheet structure.

Conclusions:

  • pH significantly dictates the aggregation pathway of human γD-Crystallin.
  • Acidic pH promotes amyloid formation, while neutral pH leads to amorphous aggregates.
  • These findings offer crucial mechanistic insights into cataractogenesis.