Interaction mechanism and compatibility studies of silk protein peptide (SPP) with the common surfactants SDS and DTAB.

The molecular interaction of low-molecular-weight SPP with common surfactants (SDS and DTAB) is a more complicated process than has been long believed. In this work, the interaction mechanism between SDS/DTAB and SPP was proposed using multiple methods including conductivity measurements, ST, UV-vis, FT-IR, DLS, fluorescence spectroscopy, and molecular docking simulations. Moreover, the foaming properties of the mixed systems were studied, and they were evaluated as cosmetics preservatives.