Unfolding, Aggregation, and Seeded Amyloid Formation of Lysine-58-Cleaved β2-Microglobulin†

Biochemistry ◽  
2005 ◽  
Vol 44 (11) ◽  
pp. 4397-4407 ◽  
Author(s):  
Niels H. H. Heegaard ◽  
Thomas J. D. Jørgensen ◽  
Noémi Rozlosnik ◽  
Dorthe B. Corlin ◽  
Jesper S. Pedersen ◽  
...  
Keyword(s):  
Amyloid Formation ◽  
Β2 Microglobulin

scholarly journals Collagen I Weakly Interacts with the β-Sheets of β2-Microglobulin and Enhances Conformational Exchange To Induce Amyloid Formation

2019 ◽  
Vol 142 (3) ◽  
pp. 1321-1331
Author(s):  
Cody L. Hoop ◽  
Jie Zhu ◽  
Shibani Bhattacharya ◽  
Caitlyn A. Tobita ◽  
Sheena E. Radford ◽  
...  
Keyword(s):  
Conformational Exchange ◽  
Collagen I ◽  
Amyloid Formation ◽  
Β2 Microglobulin ◽  
Β Sheets

Amyloid Formation under Complicated Conditions in Which β2-Microglobulin Coexists with Its Proteolytic Fragments

Biochemistry ◽  
2019 ◽  
Vol 58 (49) ◽  
pp. 4925-4934
Author(s):  
Hiroya Muta ◽  
Masatomo So ◽  
Kazumasa Sakurai ◽  
Jozsef Kardos ◽  
Hironobu Naiki ◽  
...  
Keyword(s):  
Amyloid Formation ◽  
Β2 Microglobulin ◽  
Complicated Conditions

Partially Unfolded States of β2-Microglobulin and Amyloid Formation in Vitro†

Biochemistry ◽  
2000 ◽  
Vol 39 (30) ◽  
pp. 8735-8746 ◽  
Author(s):  
Victoria J. McParland ◽  
Neil M. Kad ◽  
Arnout P. Kalverda ◽  
Anthony Brown ◽  
Patricia Kirwin-Jones ◽  
...  
Keyword(s):  
Amyloid Formation ◽  
Β2 Microglobulin ◽  
Partially Unfolded ◽  
Partially Unfolded States

A Systematic Study of the Effect of Physiological Factors on β2-Microglobulin Amyloid Formation at Neutral pH†

Biochemistry ◽  
2006 ◽  
Vol 45 (7) ◽  
pp. 2311-2321 ◽  
Author(s):  
Sarah L. Myers ◽  
Susan Jones ◽  
Thomas R. Jahn ◽  
Isobel J. Morten ◽  
Glenys A. Tennent ◽  
...  
Keyword(s):  
Systematic Study ◽  
Amyloid Formation ◽  
Physiological Factors ◽  
Β2 Microglobulin ◽  
Neutral Ph

scholarly journals Pathogenic D76N Variant of β2-Microglobulin: Synergy of Diverse Effects in Both the Native and Amyloid States

Biology ◽  
2021 ◽  
Vol 10 (11) ◽  
pp. 1197
Author(s):  
Éva Bulyáki ◽  
Judit Kun ◽  
Tamás Molnár ◽  
Alexandra Papp ◽  
András Micsonai ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Conformational Stability ◽  
Point Mutations ◽  
Amyloid Formation ◽  
Mhc I ◽  
Mutant Proteins ◽  
Β2 Microglobulin ◽  
Partial Unfolding ◽  
The Stability

β2-microglobulin (β2m), the light chain of the MHC-I complex, is associated with dialysis-related amyloidosis (DRA). Recently, a hereditary systemic amyloidosis was discovered, caused by a naturally occurring D76N β2m variant, which showed a structure remarkably similar to the wild-type (WT) protein, albeit with decreased thermodynamic stability and increased amyloidogenicity. Here, we investigated the role of the D76N mutation in the amyloid formation of β2m by point mutations affecting the Asp76-Lys41 ion-pair of WT β2m and the charge cluster on Asp38. Using a variety of biophysical techniques, we investigated the conformational stability and partial unfolding of the native state of the variants, as well as their amyloidogenic propensity and the stability of amyloid fibrils under various conditions. Furthermore, we studied the intermolecular interactions of WT and mutant proteins with various binding partners that might have in vivo relevance. We found that, relative to WT β2m, the exceptional amyloidogenicity of the pathogenic D76N β2m variant is realized by the deleterious synergy of diverse effects of destabilized native structure, higher sensitivity to negatively charged amphiphilic molecules (e.g., lipids) and polyphosphate, more effective fibril nucleation, higher conformational stability of fibrils, and elevated affinity for extracellular components, including extracellular matrix proteins.

scholarly journals Extracellular matrix components modulate different stages in β2-microglobulin amyloid formation

2019 ◽  
Vol 294 (24) ◽  
pp. 9392-9401 ◽  
Author(s):  
Núria Benseny-Cases ◽  
Theodoros K. Karamanos ◽  
Cody L. Hoop ◽  
Jean Baum ◽  
Sheena E. Radford
Keyword(s):  
Extracellular Matrix ◽  
Amyloid Formation ◽  
Β2 Microglobulin ◽  
Extracellular Matrix Components ◽  
Matrix Components

scholarly journals Specific glycosaminoglycans promote unseeded amyloid formation from β2-microglobulin under physiological conditions

2007 ◽  
Vol 72 (2) ◽  
pp. 174-181 ◽  
Author(s):  
A.J. Borysik ◽  
I.J. Morten ◽  
S.E. Radford ◽  
E.W. Hewitt
Keyword(s):  
Amyloid Formation ◽  
Physiological Conditions ◽  
Β2 Microglobulin
Sign in / Sign up

Export Citation Format

Share Document