Abstract:
:The milk protein β-lactoglobulin has been widely studied since its discovery, both as a purified protein and in mixtures with other milk proteins, where its effect on the processing properties is of importance to the dairy industry. The protein can bind a variety of small hydrophobic molecules, which may allow its use as an oral delivery vehicle. In the present study we have examined the binding of odd-numbered fatty acids by isothermal calorimetry (ITC), X-ray crystallography and computer modelling to provide a clearer picture of the extent and variability of the central binding pocket. The Kd values for the fatty acids C13, C15, C16, C17 and C19 as determined by ITC are 1.93, 2.91, 3.05, 4.11 and 8.67 × 10-7 M, respectively. The molecular structures revealed the ligands bound in the central cavity with generally well ordered lipophilic tails but significant positional variation at the carboxyl group end. In silico docking analyses identified the lipophilic interactions within the central cavity as the main driving force for binding with electrostatic interactions and H-bonds playing a minor role.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Rovoli M,Thireou T,Choiset Y,Haertlé T,Sawyer L,Eliopoulos E,Kontopidis Gdoi
10.1016/j.ijbiomac.2018.05.226subject
Has Abstractpub_date
2018-10-15 00:00:00pages
296-303issue
Pt Aeissn
0141-8130issn
1879-0003pii
S0141-8130(18)30491-4journal_volume
118pub_type
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