Possible Interaction: Lysine and Sodium Dodecyl Sulfate

“It has been found that sodium dodecyl sulfate leads to a decrease in the number of proteins/peptides containing carboxymethylated and/or carboxyethylated lysine.”

“Strong, attractive electrostatic interactions, between the anionic groups of SDS and the cationic groups of the lysines , appeared to be necessary to initiate the folding of the basic peptide.”

“Negatively charged elastin ligands, including fatty acids, bile salts or sodium dodecyl sulfate can completely inhibit the oxidation of lysine in elastin, the cationic amphiphilic ligands stimulate the enzymatic reaction five-fold, while small hydrophilic molecules of either charge or neutral detergents have no effect.”

“The Lysines have no effect on peptide solubility in SDS and on peptide secondary structure, but they abolish peptide dimerization on SDS gels.”

“In most of the intact proteins (B proteins), most of which contained disulfide bridges, helicity in SDS decreased with an increase in Lys fraction.”

“It was found that sodium dodecyl sulfate was bound to some of the ϵ-amino groups of lysine in bovine serum albumin, ovalbumin, and human γ-globulin and rendered the involved amino groups unreactive toward TNBS.”