Kinetics of amyloid aggregation of mammal apomyoglobins and correlation with their amino acid sequences.
In protein deposition disorders, a normally soluble protein is deposited as insoluble aggregates, referred to as amyloid. The intrinsic effects of specific mutations on the rates of protein aggregation and amyloid formation of unfolded polypeptide chains can be correlated with changes in hydrophobicity, propensity to convert alpha-helical to beta sheet conformation and charge. In this paper, we report the aggregation rates of buffalo, horse and bovine apomyoglobins. The experimental values were compared with the theoretical ones evaluated considering the amino acid differences among the sequences. Our results show that the mutations which play critical roles in the rate-determining step of apomyoglobin aggregation are those located within the N-terminal region of the molecule.
Vilasi
Silvia
S
Dipartimento di Biochimica e Biofisica, Seconda Università degli Studi di Napoli, Via L. De Crecchio 7, 80138 Naples, Italy.
Dosi
Roberta
R
Iannuzzi
Clara
C
Malmo
Clorinda
C
Parente
Augusto
A
Irace
Gaetano
G
Sirangelo
Ivana
I
D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry* / Q000235:genetics; D000818:Animals; D001059:Apoproteins / Q000737:chemistry* / Q000235:genetics; D002020:Buffaloes; D002417:Cattle; D006736:Horses; D007700:Kinetics; D008969:Molecular Sequence Data; D009211:Myoglobin / Q000737:chemistry* / Q000235:genetics; D017433:Protein Structure, Secondary
D000682:Amyloid; D001059:Apoproteins; D009211:Myoglobin; C010857:apomyoglobin