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

Otte, J; Ipsen, R; Bauer, R; Bjerrum, MJ and Waninge, Rianne LU (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)
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author
organization
publishing date
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
2007-08-13 14:05:02
date last changed
2017-04-30 14:08:47
@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},
  keyword      = {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},
  volume       = {15},
  year         = {2005},
}