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.
Badraghi
Jalil
J
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
Moosavi-Movahedi
Ali Akbar
AA
Saboury
Ali Akbar
AA
Yousefi
Reza
R
Sharifzadeh
Ahmad
A
Hong
Jun
J
Haertlé
Thomas
T
Niasari-Naslaji
Amir
A
Sheibani
Nader
N
D000818:Animals; D002021:Buffers; D002162:Camelus; D002364:Caseins / Q000737:chemistry*; D002942:Circular Dichroism; D004229:Dithiothreitol / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D007328:Insulin / Q000737:chemistry / Q000378:metabolism*; D008892:Milk / Q000378:metabolism; D018832:Molecular Chaperones / Q000737:chemistry*; D011485:Protein Binding; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry*; D055672:Static Electricity; D013997:Time Factors; D014466:Ultraviolet Rays
D002021:Buffers; D002364:Caseins; D007328:Insulin; D018832:Molecular Chaperones; D012967:Sodium Dodecyl Sulfate; D004229:Dithiothreitol