Abstract:
:Hydrogen-Deuterium exchange kinetics of β-lactoglobulin and β-lactoglobulin (-)-epicatechin solutions has been investigated through the analysis of the amide I absorption band at 1650cm-1 in the FTIR spectrum. H-D substitution in NH amides and residues of the protein results in a slight red-shift and in intensity changes of the amide I components: either these effects have been inspected in the framework of the Principal Components Analysis methods. The present analysis allowed to unveil three H-D kinetics at the timescale of the oligomeric fluctuations of the protein. A fast mechanism (lifetime from 5 to 10min) can be ascribed to the dynamics of protein oligomers and aggregates at the scale of the quaternary structure variations, and it is not observed in the complexes β-lactoglobulin (-)-epicatechin. The other slowest kinetics, whose lifetimes are in the range 1-10h, are here associated to dynamics of high-molecular weight complexes that hamper the proton exchange. The role of (-)-epicatechin as an enhancer of the formation of stable high-molecular weight aggregates from β-lactoglobulin is also discussed by comparison of the lifetimes at different protein concentrations.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Caporaletti F,Carbonaro M,Maselli P,Nucara Adoi
10.1016/j.ijbiomac.2017.06.028subject
Has Abstractpub_date
2017-11-01 00:00:00pages
521-526issue
Pt Aeissn
0141-8130issn
1879-0003pii
S0141-8130(17)30356-2journal_volume
104pub_type
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