Aggregation of trypsin and trypsin inhibitor by Al cation

P. Chanphai, L. Kreplak, H. A. Tajmir-Riahi

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7 Citas (Scopus)

Resumen

Al cation may trigger protein structural changes such as aggregation and fibrillation, causing neurodegenerative diseases. We report the effect of Al cation on the solution structures of trypsin (try) and trypsin inhibitor (tryi), using thermodynamic analysis, UV–Visible, Fourier transform infrared (FTIR) spectroscopic methods and atomic force microscopy (AFM). Thermodynamic parameters showed Al-protein bindings occur via H-bonding and van der Waals contacts for trypsin and trypsin inhibitor. AFM showed that Al cations are able to force trypsin into larger or more robust aggregates than trypsin inhibitor, with trypsin 5 ± 1 SE (n = 52) proteins per aggregate and for trypsin inhibitor 8.3 ± 0.7 SE (n = 118). Thioflavin T test showed no major protein fibrillation in the presence of Al cation. Al complexation induced more alterations of trypsin inhibitor conformation than trypsin.

Idioma originalEnglish
Páginas (desde-hasta)7-12
Número de páginas6
PublicaciónJournal of Photochemistry and Photobiology B: Biology
Volumen169
DOI
EstadoPublished - abr. 1 2017

Nota bibliográfica

Funding Information:
This work is supported by grant from Natural Sciences and Engineering Research Council of Canada (NSERC).

Publisher Copyright:
© 2017 Elsevier B.V.

ASJC Scopus Subject Areas

  • Radiation
  • Radiological and Ultrasound Technology
  • Biophysics
  • Radiology Nuclear Medicine and imaging

PubMed: MeSH publication types

  • Journal Article

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