Strong acids induce amyloid fibril formation of β2-microglobulin via an anion-binding mechanism
K. Yamaguchi, Kenshiro Hasuo, Masatomo So, Kensuke Ikenaka, Hideki Mochizuki, Yuji Goto
Abstract
. Although trichloroacetic acid, another strong acid, promoted amyloid fibril formation of β2m, formic acid, a weak acid, did not, suggesting the dominant role of anions in promoting fibril formation of this protein. Comparison of the effects of acids and salts confirmed the critical role of anions, indicating that strong acids likely induce amyloid fibril formation via an anion-binding mechanism. The results suggest that although the addition of strong acids decreases pH, it is not useful for degrading amyloid fibrils, but rather induces or stabilizes amyloid fibrils via an anion-binding mechanism.
Topics & Concepts
FibrilChemistryAmyloid (mycology)Beta-2 microglobulinAmino acidAmyloid diseaseBiophysicsAmyloid fibrilBiochemistryFormic acidAmyloid βBiologyInorganic chemistryDiseaseImmunologyPathologyMedicineAlzheimer's disease research and treatmentsPrion Diseases and Protein MisfoldingProtein Structure and Dynamics