1. Kinetics of amyloid aggregation of mammal apomyoglobins and correlation with their amino acid sequences
- Author
-
Clara Iannuzzi, Ivana Sirangelo, Augusto Parente, Gaetano Irace, Silvia Vilasi, Clorinda Malmo, Roberta Dosi, Vilasi, S, Dosi, R, Iannuzzi, Clara, Malmo, C, Parente, A, Irace, Gaetano, and Sirangelo, Ivana
- Subjects
Amyloid ,Buffaloes ,Kinetics ,Molecular Sequence Data ,Biophysics ,Beta sheet ,Protein aggregation ,Biochemistry ,Protein Structure, Secondary ,chemistry.chemical_compound ,Structural Biology ,Genetics ,Molecule ,Animals ,Amino Acid Sequence ,Horses ,Molecular Biology ,chemistry.chemical_classification ,Chemistry ,Myoglobin ,Cell Biology ,Amino acid ,Protein aggregation rate ,Amyloid aggregation ,Apomyoglobin aggregation ,Cattle ,Apoproteins - Abstract
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 α-helical to β 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.
- Published
- 2006