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Citation
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HERO ID
1039177
Reference Type
Journal Article
Title
The formation of amyloid-like fibrils of α-chymotrypsin in different aqueous organic solvents
Author(s)
Simona, LM; Laczkób, I; Demcsáka, A; Tótha, D; Kotormán, M; Fülöp, L
Year
In Press
Is Peer Reviewed?
1
Journal
Protein and Peptide Letters
ISSN:
0929-8665
EISSN:
1875-5305
Language
English
PMID
22185498
Abstract
The formation of amyloid-like fibrils of α-chymotrypsin was studied in aqueous ethanol, methanol, tert-butanol, 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 °C 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 α-chymotrypsin. The ThT, CR binding and far-UV CD measurements indicated that the formation of the cross- structure of α-chymotrypsin depends on the polarity of the organic solvent. To determine the role of surface charges in the aggregation, chemically modified forms of α-chymotrypsin 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 α-chymotrypsin.
Tags
IRIS
•
tert-Butanol
Considered Studies
Electronic Search
Excluded/ Not on Topic
Methodology/Solvent
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