Work

Assembly of Hydrophobin class I from Agaricus bisporus produced different amyloid-like fibrils

Year: 2024

Type: article

Abstract: . ThT experiments demonstrated that the production of fibrils decreased at basic pH, while acidic and neutral pH favoured the formation of fibrils. Likewise, the addition of colloidal Teflon affects the formation of fibrils. Circular dichroism spectra proved that hydrophobin class I undergo changes in its secondary structure, increasing its alpha helix and beta sheet content after vortexing. It was observed that the analysis by scanning electron microscopy and atomic force microscopy of the hydrophobin produced different amyloid-like structures in glass and mica.

Source: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

DOI: 10.1016/j.bbapap.2024.141048

Authors: Jesús Rojas-Osnaya, Hugo Nájera

Institution: Universidad Autónoma Metropolitana

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,730

Funder: Consejo Nacional de Ciencia y Tecnología