Document Detail

Bovine serum albumin oligomers in the E- and B-forms at low protein concentration and ionic strength.
MedLine Citation:
PMID:  23148944     Owner:  NLM     Status:  MEDLINE    
The manuscript describes the study of the oligomerization process of bovine serum albumin (BSA) in two different structural monomeric forms: the extended-form (E) at pH 2.0 and the basic-form (B) at pH 9.0. The study was conducted at low protein concentration (1mg/ml) and relatively short incubation time (maximum 56 days) in order to investigate early oligomerization events rather than the formation of mature fibrils. The comparison between the two isoforms show that oligomers form much faster (∼6 days) in the E-form than in the B-form where formation of oligomers requires ∼4 weeks. The oligomers appear to be limited to a maximum of tetramers with size <30 nm. Hydrophobic interactions from exposed neutral amino acid residues in the elongated E-form are the likely cause for the quick formation of aggregates at acidic pH. We used an array of biophysical techniques for the study and determined that oligomerization occurs without further large changes in the secondary structure of the monomers. Under the conditions adopted in this study, aggregation does not seem to exceed the formation of tetramers, even though a very small amount of much larger aggregates seem to form.
Jeremiah J Babcock; Lorenzo Brancaleon
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2012-11-10
Journal Detail:
Title:  International journal of biological macromolecules     Volume:  53     ISSN:  1879-0003     ISO Abbreviation:  Int. J. Biol. Macromol.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2012-12-25     Completed Date:  2013-06-04     Revised Date:  2014-02-04    
Medline Journal Info:
Nlm Unique ID:  7909578     Medline TA:  Int J Biol Macromol     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  42-53     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Elsevier B.V. All rights reserved.
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MeSH Terms
Amyloid / chemistry
Circular Dichroism
Hydrogen-Ion Concentration
Microscopy, Atomic Force
Models, Molecular
Particle Size
Protein Multimerization
Protein Stability
Protein Structure, Quaternary
Protein Structure, Secondary
Scattering, Radiation
Serum Albumin, Bovine / chemistry*,  ultrastructure
Spectrometry, Fluorescence
Grant Support
2G12RR013646-11/RR/NCRR NIH HHS; G12 RR013646/RR/NCRR NIH HHS
Reg. No./Substance:
0/Amyloid; 0/Serum Albumin, Bovine; 0/Solutions

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