Back to Search
Start Over
Recombinant Bri3 BRICHOS domain is a molecular chaperone with effect against amyloid formation and non-fibrillar protein aggregation
- Source :
- Scientific Reports, Scientific Reports, Vol 10, Iss 1, Pp 1-14 (2020)
- Publication Year :
- 2020
-
Abstract
- Molecular chaperones assist proteins in achieving a functional structure and prevent them from misfolding into aggregates, including disease-associated deposits. The BRICHOS domain from familial dementia associated protein Bri2 (or ITM2B) probably chaperones its specific proprotein region with high β-sheet propensity during biosynthesis. Recently, Bri2 BRICHOS activity was found to extend to other amyloidogenic, fibril forming peptides, in particular, Alzheimer’s disease associated amyloid-β peptide, as well as to amorphous aggregate forming proteins. However, the biological functions of the central nervous system specific homologue Bri3 BRICHOS are still to be elucidated. Here we give a detailed characterisation of the recombinant human (rh) Bri3 BRICHOS domain and compare its structural and functional properties with rh Bri2 BRICHOS. The results show that rh Bri3 BRICHOS forms more and larger oligomers, somewhat more efficiently prevents non-fibrillar protein aggregation, and less efficiently reduces Aβ42 fibril formation compared to rh Bri2 BRICHOS. This suggests that Bri2 and Bri3 BRICHOS have overlapping molecular mechanisms and that their apparently different tissue expression and processing may result in different physiological functions.
- Subjects :
- Models, Molecular
Protein Denaturation
Amyloid
Protein domain
lcsh:Medicine
Peptide
Nerve Tissue Proteins
Protein aggregation
Fibril
Biochemistry
Article
law.invention
Protein Aggregates
Protein Domains
law
Chaperones
Humans
Amino Acid Sequence
Proprotein
lcsh:Science
Peptide sequence
chemistry.chemical_classification
Multidisciplinary
Amyloid beta-Peptides
lcsh:R
Membrane Proteins
Proteins
Peptide Fragments
Recombinant Proteins
Cell biology
Kinetics
chemistry
Recombinant DNA
lcsh:Q
Subjects
Details
- ISSN :
- 20452322
- Volume :
- 10
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Scientific reports
- Accession number :
- edsair.doi.dedup.....9259b72a00faec599b805a6a3188ae1f