The formation of amyloid-like fibrils of αchymotrypsin in different aqueous organic solvents

L. Mária Simon, Ilona Laczkó, Anett Demcsák, Dávid Tóth, Márta Kotormán, Lívia Fülöp

Research output: Article

10 Citations (Scopus)

Abstract

The formation of amyloid-like fibrils of αchymotrypsin was studied in aqueous ethanol, methanol, tertbutanol, dimethylformamide and acetonitrile. Thioflavin T (ThT), Congo red (CR) and 1-anilino-8-naphthalenesulfonic acid (ANS) binding, turbidity, intrinsic fluorescence and far-UV circular dichroism measurements were employed to characterize the amyloid fibril formation. The greatest extent of fibril formation after incubation for 24 h at pH 7.0 and at 24 oC was in ethanol at 55%, in methanol and dimethylformamide (DMF) at 60-70% and in tert-butanol at 60-80%. The ANS binding and intrinsic fluorescence results showed that the hydrophobic residues are more solvent-exposed in the aggregated form of αchymotrypsin. The ThT, CR binding and far-UV CD measurements indicated that the formation of the cross-β structure of αchymotrypsin depends on the polarity of the organic solvent. To determine the role of surface charges in the aggregation, chemically modified forms of αchymotrypsin were prepared. The citraconylated and succinylated enzymes exhibited a higher and the enzyme forms modified with aliphatic aldehydes a lower propensity for aggregation. These results suggest the important role of surface charges in the aggregation of αchymotrypsin.

Original languageEnglish
Pages (from-to)544-550
Number of pages7
JournalProtein and Peptide Letters
Volume19
Issue number5
DOIs
Publication statusPublished - máj. 1 2012

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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