Structure and stability analysis of cytotoxic complex of camel α-lactalbumin and unsaturated fatty acids produced at high temperature.

α-Lactalbumin α-La), together with oleic acid can be converted to a complex, which kills tumor cells selectively. Cytotoxic α-La -oleic acid and α-La -linoleic acid complexes were generated by adding fatty acid to camel holo α-La at 60 ° C (referred to as La-OA-60 and La-LA-60 state, respectively). Structural properties of these complexes were studied and compared to the camel α-La.

Dual behavior of sodium dodecyl sulfate as enhancer or suppressor of insulin aggregation and chaperone-like activity of camel alphaS(1)-casein.

Sodium dodecyl sulfate (SDS) at low concentrations considerably enhanced insulin aggregation and reduced the chaperone-like activity of purified camel alphaS(1)-casein (alphaS(1)-CN). These observed changes were the result of repulsive electrostatic interactions between both negative charged head groups of SDS and alphaS(1)-CN, and the net negative charge of insulin molecules, resulting in the greater exposure of hydrophobic patches of insulin and its enhanced aggregation. In contrast, enhanced hydrophobic interactions were primarily responsible for the conformational changes observed in insulin and alphaS(1)-CN at high SDS concentrations, resulting in increased binding of SDS and alphaS(1)-CN to insulin and its reduced aggregation.

Effect of salts and sodium dodecyl sulfate on chaperone activity of camel alphaS(1)-CN: insulin as the target protein.

In this study camel alphaS(1)-casein (alphaS(1)-CN) was purified, using a two-step purification procedure. The anti-aggregation (chaperone-like) ability of the purified protein sample was examined in a wide range of experimental conditions and at different concentrations of camel alphaS(1)-CN, in the presence of salts and sodium dodecyl sulfate (SDS). To examine chaperone-like activity of camel alphaS(1)-CN, bovine pancreatic insulin was used as the target protein.

Chaperone activities of bovine and camel beta-caseins: Importance of their surface hydrophobicity in protection against alcohol dehydrogenase aggregation.

Beta-casein (beta-CN) showing properties of intrinsically unstructured proteins (IUP) displays many similarities with molecular chaperones and shows anti-aggregation activity in vitro. Chaperone activities of bovine and camel beta-CN were studied using alcohol dehydrogenase (ADH) as a substrate. To obtain an adequate relevant information about the chaperone capacities of studied caseins, three different physical parameters including chaperone constant (k(c), microM(-1)), thermal aggregation constant (k(T), degrees C(-1)) and aggregation rate constant (k(t), min(-1)) were measured.