Effects of Triton X-100 nanoaggregates on dimerization and antioxidant activity of morin

Dimerization and antioxidant activity of morin in the Triton X-100 micelles were studied by electronic absorption, ATR-FTIR spectra, cyclic voltammetric, DSC, freeze-fracture TEM, molecular modeling and ab initio quantum calculations. Morin can be solubilized in the Triton X-100 micelles and show selective dimerization in Triton X-100 micelles with different structures. In Triton X-100 spherical micelles, morin always exists in the form of dimer, and in Triton X-100 rodlike micelles, it is always in the form of monomer. The solubilization of morin dimer in Triton X-100 spherical micelles changes the micelle morphology from spherical to cubelike, and the size of the single micelle is also increased, while morin monomer links the Triton X-100 rodlike micelles and forms a kind of network micelle structure with the size of the "rod" unchanged. Solubilized and concentrated in Triton X-100 micelles, morin can protect human serum albumin from the damage induced by hydroxyl radicals effectively and even can form a kind of protein complex with human serum albumin showing more thermal stability.