Formation of amyloid-like fibrils upon limited proteolysis of bovine α-lactalbumin

Research output: Contribution to journal › Journal article › Research › peer-review

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Formation of amyloid-like fibrils upon limited proteolysis of bovine α-lactalbumin. / Otte, Jeanette; Ipsen, Richard; Bauer, Rogert; Bjerrum, Morten J.; Waninge, Rianne.

In: International Dairy Journal, Vol. 15, No. 3, 2005, p. 219-229.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Otte, J, Ipsen, R, Bauer, R, Bjerrum, MJ & Waninge, R 2005, 'Formation of amyloid-like fibrils upon limited proteolysis of bovine α-lactalbumin', International Dairy Journal, vol. 15, no. 3, pp. 219-229. https://doi.org/10.1016/j.idairyj.2004.07.004

APA

Otte, J., Ipsen, R., Bauer, R., Bjerrum, M. J., & Waninge, R. (2005). Formation of amyloid-like fibrils upon limited proteolysis of bovine α-lactalbumin. International Dairy Journal, 15(3), 219-229. https://doi.org/10.1016/j.idairyj.2004.07.004

Vancouver

Otte J, Ipsen R, Bauer R, Bjerrum MJ, Waninge R. Formation of amyloid-like fibrils upon limited proteolysis of bovine α-lactalbumin. International Dairy Journal. 2005;15(3):219-229. https://doi.org/10.1016/j.idairyj.2004.07.004

Author

Otte, Jeanette ; Ipsen, Richard ; Bauer, Rogert ; Bjerrum, Morten J. ; Waninge, Rianne. / Formation of amyloid-like fibrils upon limited proteolysis of bovine α-lactalbumin. In: International Dairy Journal. 2005 ; Vol. 15, No. 3. pp. 219-229.

Bibtex

@article{b78ab2b4d0db4d6d8cac477a93d8bc32,
title = "Formation of amyloid-like fibrils upon limited proteolysis of bovine α-lactalbumin",
abstract = "Bovine α-lactalbumin (α-LA) (10 g L-1) was incubated with a protease from Bacillus licheniformis at pH 7.5 and 50°C. The reaction was biphasic consisting of an initial hydrolysis of intact α-LA and formation of dimers from large hydrolysis products within 60 min followed by aggregation of dimers into aggregates of 500 kDa. The aggregates consisted primarily of fibrillar strands with a diameter of 5 nm. Formation of these strands was accompanied by a change in secondary structure towards higher β-sheet content and strong binding of thioflavin, features shared with amyloidal fibrils. The main components in these fibrils were fragments of 8.8 and 9.8 kDa shown to occur in a monomer-dimer equilibrium. These fragments were identified and a molecular mechanism involving side-by-side assembly of dimers of these fragments into fibrils is proposed.",
keywords = "α-Lactalbumin, Amyloid fibrils, Assembly, Fragments, Proteolysis",
author = "Jeanette Otte and Richard Ipsen and Rogert Bauer and Bjerrum, {Morten J.} and Rianne Waninge",
year = "2005",
doi = "10.1016/j.idairyj.2004.07.004",
language = "English",
volume = "15",
pages = "219--229",
journal = "International Dairy Journal",
issn = "0958-6946",
publisher = "Elsevier",
number = "3",

}

RIS

TY - JOUR

T1 - Formation of amyloid-like fibrils upon limited proteolysis of bovine α-lactalbumin

AU - Otte, Jeanette

AU - Ipsen, Richard

AU - Bauer, Rogert

AU - Bjerrum, Morten J.

AU - Waninge, Rianne

PY - 2005

Y1 - 2005

N2 - Bovine α-lactalbumin (α-LA) (10 g L-1) was incubated with a protease from Bacillus licheniformis at pH 7.5 and 50°C. The reaction was biphasic consisting of an initial hydrolysis of intact α-LA and formation of dimers from large hydrolysis products within 60 min followed by aggregation of dimers into aggregates of 500 kDa. The aggregates consisted primarily of fibrillar strands with a diameter of 5 nm. Formation of these strands was accompanied by a change in secondary structure towards higher β-sheet content and strong binding of thioflavin, features shared with amyloidal fibrils. The main components in these fibrils were fragments of 8.8 and 9.8 kDa shown to occur in a monomer-dimer equilibrium. These fragments were identified and a molecular mechanism involving side-by-side assembly of dimers of these fragments into fibrils is proposed.

AB - Bovine α-lactalbumin (α-LA) (10 g L-1) was incubated with a protease from Bacillus licheniformis at pH 7.5 and 50°C. The reaction was biphasic consisting of an initial hydrolysis of intact α-LA and formation of dimers from large hydrolysis products within 60 min followed by aggregation of dimers into aggregates of 500 kDa. The aggregates consisted primarily of fibrillar strands with a diameter of 5 nm. Formation of these strands was accompanied by a change in secondary structure towards higher β-sheet content and strong binding of thioflavin, features shared with amyloidal fibrils. The main components in these fibrils were fragments of 8.8 and 9.8 kDa shown to occur in a monomer-dimer equilibrium. These fragments were identified and a molecular mechanism involving side-by-side assembly of dimers of these fragments into fibrils is proposed.

KW - α-Lactalbumin

KW - Amyloid fibrils

KW - Assembly

KW - Fragments

KW - Proteolysis

U2 - 10.1016/j.idairyj.2004.07.004

DO - 10.1016/j.idairyj.2004.07.004

M3 - Journal article

AN - SCOPUS:12344306647

VL - 15

SP - 219

EP - 229

JO - International Dairy Journal

JF - International Dairy Journal

SN - 0958-6946

IS - 3

ER -

ID: 226823565