The role of protein stability, solubility, and net charge in amyloid fibril formation

Protein Science : a Publication of the Protein Society
Jason P Schmittschmitt, J Martin Scholtz

Abstract

Ribonuclease Sa and two charge-reversal variants can be converted into amyloid in vitro by the addition of 2,2,2-triflouroethanol (TFE). We report here amyloid fibril formation for these proteins as a function of pH. The pH at maximal fibril formation correlates with the pH dependence of protein solubility, but not with stability, for these variants. Additionally, we show that the pH at maximal fibril formation for a number of well-characterized proteins is near the pI, where the protein is expected to be the least soluble. This suggests that protein solubility is an important determinant of fibril formation.

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Related Concepts

Thioflavine
Ribonuclease Sa2
Amyloid Fibrils
Circular Dichroism, Vibrational
Enzyme Stability
Hydrogen-Ion Concentration
Alloenzymes
Plasma Protein Binding Capacity
Protein Conformation
Protein Denaturation

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