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 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

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 Heating during agitation of β2-microglobulin reveals that supersaturation breakdown is required for amyloid fibril formation at neutral pH

2019 ◽  
Vol 294 (43) ◽  
pp. 15826-15835 ◽  
Author(s):  
Masahiro Noji ◽  
Kenji Sasahara ◽  
Keiichi Yamaguchi ◽  
Masatomo So ◽  
Kazumasa Sakurai ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Β2 Microglobulin ◽  
Neutral Ph ◽  
Amyloid Fibril Formation

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

Bactericidal Effect of Lactoferrin and Its Amidated and Pepsin-Digested Derivatives on Pseudomonasfluorescens: Influence of Environmental and Physiological Factors

2008 ◽  
Vol 71 (12) ◽  
pp. 2468-2474 ◽  
Author(s):  
ANA del OLMO ◽  
PILAR MORALES ◽  
MANUEL NUÑEZ
Keyword(s):  
Complex Systems ◽  
Bactericidal Activity ◽  
Phosphate Buffer ◽  
Bactericidal Effect ◽  
Bovine Lactoferrin ◽  
Medium Ph ◽  
Physiological Factors ◽  
Pepsin Digestion ◽  
Neutral Ph ◽  
Bacterial Inoculum

The influence of environmental and physiological factors such as substrate composition and inoculum characteristics on the bactericidal activity of bovine lactoferrin (LF) and its amidated and pepsin-digested derivatives against Pseudomonasfluorescens was investigated. Amidated LF (AMILF) exerted the most potent bactericidal activity, with a 5.8-log decrease in P.fluorescens counts, and LF the lowest, with just a 1-log decrease, whereas pepsin-digested LF (PDLF) reduced bacterial counts by 2.7 log, after 1 h at 30°C. Amidation of PDLF increased effectiveness by 1.2 log, whereas pepsin digestion of AMILF decreased effectiveness by 2.8 log. Bactericidal activity of LF and its derivatives was higher in Tris buffer than in phosphate buffer. The bactericidal effect of AMILF and PDLF was enhanced as medium pH was increased from 5.5 to 8.5, whereas LF showed higher activity under acidic or basic conditions than at neutral pH. The presence of cations affected the activity of LF and its derivatives, from a concentration of 10 mM for K+, 1 mM for Na+, and 0.1 mM for Ca2+,Co2+,Cu2+, Mg2+,Zn2+, and Fe3+. Bactericidal effectiveness diminished as the bacterial inoculum was increased. Log-phase cultures (10-h incubation) were less sensitive to the bactericidal activity of LF and its derivatives than stationary cultures (20- and 30-h incubation). All these factors should be considered when applications of LF and its derivatives in foods and other complex systems are investigated.

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

Apolipoprotein E Inhibits the Depolymerization of β2-Microglobulin-Related Amyloid Fibrils at a Neutral pH†

Biochemistry ◽  
2001 ◽  
Vol 40 (29) ◽  
pp. 8499-8507 ◽  
Author(s):  
Itaru Yamaguchi ◽  
Kazuhiro Hasegawa ◽  
Naoki Takahashi ◽  
Fumitake Gejyo ◽  
Hironobu Naiki
Keyword(s):  
Apolipoprotein E ◽  
Amyloid Fibrils ◽  
Β2 Microglobulin ◽  
Neutral Ph

How Post-Translational Modifications Influence Amyloid Formation: A Systematic Study of Phosphorylation and Glycosylation in Model Peptides

2010 ◽  
Vol 16 (26) ◽  
pp. 7881-7888 ◽  
Author(s):  
Malgorzata Broncel ◽  
Jessica A. Falenski ◽  
Sara C. Wagner ◽  
Christian P. R. Hackenberger ◽  
Beate Koksch
Keyword(s):  
Systematic Study ◽  
Amyloid Formation ◽  
Post Translational Modifications ◽  
Model Peptides
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