Formation of amyloid-like fibrils upon limited proteolysis of bovine alpha-lactalbumin
(2005) In International Dairy Journal 15(3). p.219-229- Abstract
- Bovine alpha-lactalbumin (alpha-LA) (10 g L-1) was incubated with a protease from Bacillus licheniformis at pH 7.5 and 50 degreesC. The reaction was biphasic consisting of an initial hydrolysis of intact alpha-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 beta-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... (More)
- Bovine alpha-lactalbumin (alpha-LA) (10 g L-1) was incubated with a protease from Bacillus licheniformis at pH 7.5 and 50 degreesC. The reaction was biphasic consisting of an initial hydrolysis of intact alpha-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 beta-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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/254475
- author
- Otte, J ; Ipsen, R ; Bauer, R ; Bjerrum, MJ and Waninge, Rianne LU
- organization
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- amyloid fibrils, assembly, fragments, alpha-lactalbumin, proteolysis
- in
- International Dairy Journal
- volume
- 15
- issue
- 3
- pages
- 219 - 229
- publisher
- Elsevier
- external identifiers
-
- wos:000226911800003
- scopus:12344306647
- ISSN
- 0958-6946
- DOI
- 10.1016/j.idairyj.2004.07.004
- language
- English
- LU publication?
- yes
- id
- e31a3411-73ed-4675-afed-90cfdcc114d9 (old id 254475)
- date added to LUP
- 2016-04-01 16:21:58
- date last changed
- 2023-12-13 07:54:58
@article{e31a3411-73ed-4675-afed-90cfdcc114d9,
abstract = {{Bovine alpha-lactalbumin (alpha-LA) (10 g L-1) was incubated with a protease from Bacillus licheniformis at pH 7.5 and 50 degreesC. The reaction was biphasic consisting of an initial hydrolysis of intact alpha-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 beta-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.}},
author = {{Otte, J and Ipsen, R and Bauer, R and Bjerrum, MJ and Waninge, Rianne}},
issn = {{0958-6946}},
keywords = {{amyloid fibrils; assembly; fragments; alpha-lactalbumin; proteolysis}},
language = {{eng}},
number = {{3}},
pages = {{219--229}},
publisher = {{Elsevier}},
series = {{International Dairy Journal}},
title = {{Formation of amyloid-like fibrils upon limited proteolysis of bovine alpha-lactalbumin}},
url = {{http://dx.doi.org/10.1016/j.idairyj.2004.07.004}},
doi = {{10.1016/j.idairyj.2004.07.004}},
volume = {{15}},
year = {{2005}},
}