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