Possible Interaction: Sodium Dodecyl Sulfate and Trypsin

“Curiously, TI dimerizes in the presence of SDS , a feature which has been observed previously only in non-denaturing gels of human alpha 1-antitrypsin (alpha 1PI).”

“Exposure of trypsin to SDS at a molar ratio of 1:45 led to decrease in trypsin activity by 61%.”

“the disaccharides trehalose and sucrose, in the stabilization of bovine trypsin against exposure to the anionic detergent sodium dodecyl sulfate and autolysis.”

“ Trypsin treatment of vesicles causes complete loss of the 300 K spanning protein from SDS gels while dot blots show that some but not all the antigenic activity is lost.”

“The effect of SDS on trypsin digestion in terms of the number of peptides generated and the overall protein sequence coverage by these peptides is found to be protein dependent.”

“Circular dichroism spectra show the high alpha-helical content and unfolded structure of trypsin in the presence of SDS due to strong electrostatic repulsion leading to a probable "necklace and bead" model in the case of biopolymer-surfactant complexes.”

“When the larger complex was isolated by electroelution from a sodium dodecyl sulfate gel and treated with trypsin , a species corresponding to Mr = 100,000 was generated.”

“Following conjugation, the stability of trypsin in the presence of protein denaturants such as urea and sodium dodecyl sulfate was markedly increased, and the enzyme became resistant to inhibition by naturally-occurring protease inhibitors [2,3] .”

“Molecular dynamic simulations showed that treatment with SDS resulted in the structure of trypsin becoming unstable and unfolded near its active center.”

“This work provides insights into the interaction of SDS with trypsin on the molecular level and is beneficial to understanding of how SDS affects the conformation and activity of trypsin in application processes.”

“To determine the mechanism by which the interaction of SDS influences the structure and activity of trypsin , molecular docking, molecular dynamics simulations, DSC, and multi-spectroscopic measures including UV absorption, fluorescence, and circular dichroism were used.”

“The spectroscopic techniques show the change of the conformation, i.e., the … of the values of alpha-helicity, beta-sheet, and random-coil of trypsin in the presence of SDS , and ultimately unfolding of trypsin occurs due to strong electrostatic repulsion of micellar clusters of the protein-surfactant complexes.”

“In addition, modification protected trypsin against denaturation in the presence of sodium dodecylsulfate.”