Comparative analysis of the interaction between azobenzene di-maleimide and human serum albumin/lysozyme

Y Interactions between 4,4'-bis(maleimido)azobenzene and human serum albumin/lysozyme were investigated using fluorescence and computational methods to determine how the azobenzene compound participates in protein transmission and distribution. Fluorescence titration and time-resolved fluorescence revealed that the binding of 4,4'-bis(maleimido)azobenzene to human serum albumin/lysozyme was a static quenching with 105 middle-affinity, and the lysozyme system was easily affected by temperature. The binding was spontaneous and driven by hydrogen bonding and van der Waals forces. Molecular docking results indicated that the azobenzene was mainly inserted into the active site I of human serum albumin and bound near the active sites of tryptophan 62 and 63 amino acid residues in lysozyme. Conformation research revealed that the secondary structure of the proteins and the hydrophobic environment around tryptophan residues were substantially changed compared with those in human serum albumin, this result was confirmed by three-dimensional spectroscopy. Therefore, the number of active sites in different positions seriously influences the transportation and distribution of the azobenzene di-maleimide to human serum albumin/lysozyme. (C) 2021 Elsevier B.V. All rights reserved.

Automated summary

The study found that the interaction between 4,4'-bis(maleimido)azobenzene and human serum albumin/lysozyme is mainly through static quenching, driven by hydrogen bonding and van der Waals forces, with lysozyme being more temperature sensitive. The binding of azobenzene within the proteins leads to significant changes in their secondary structures and the hydrophobic environment around active sites, impacting the transportation and distribution of the compound.