Modulating weak protein-protein cross-interactions by addition of free amino acids at millimolar concentrations
arxiv(2024)
摘要
In this paper, we quantify weak protein protein interactions in solution
using Cross-Interaction Chromatography (CIC) and Surface Plasmon Resonance
(SPR) and demonstrate that they can be modulated by the addition of free amino
acids. With CIC, we determined the second osmotic virial cross-interaction
coefficient (B23) as a proxy for the interaction strength between two different
proteins. We perform SPR experiments to establish the binding affinity between
the same proteins. With CIC, we show that the amino acids proline, glutamine,
and arginine render the protein cross-interactions more repulsive or
equivalently less attractive. Specifically, we measured B23 between lysozyme
(Lys) and bovine serum albumin (BSA) and between Lys and protein isolates (whey
and canola). We find that B23 increases when amino acids are added to the
solution even at millimolar concentrations, corresponding to protein ligand
stoichiometric ratios as low as 1 to 1. With SPR, we show that the binding
affinity between proteins can change by one order of magnitude when 10 mM of
glutamine are added. In the case of Lys and one whey protein isolate it changes
from the mM to the M, thus by three orders of magnitude. Interestingly, this
efficient modulation of the protein cross-interactions does not alter the
protein's secondary structure. The capacity of amino acids to modulate protein
cross-interactions at mM concentrations is remarkable and may have an impact
across fields in particular for specific applications in the food or
pharmaceutical industries.
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