Capturing the interaction potential of amyloidogenic proteins.
Experimentally derived static structure factors obtained for the aggregation-prone protein insulin were analyzed with a statistical mechanical model based on the Derjaguin-Landau-Verwey-Overbeek potential. The data reveal that the protein self-assembles into equilibrium clusters already at low concentrations. Furthermore, striking differences regarding interaction forces between aggregation-prone proteins such as insulin in the preaggregated regime and natively stable globular proteins are found.
University of Dortmund, Department of Chemistry, Physical Chemistry I-Biophysical Chemistry, Otto-Hahn Strasse 6, D-44227 Dortmund, Germany.
Nadeem
N
Javid
Karsten
K
Vogtt
Christina
C
Krywka
Metin
M
Tolan
Roland
R
Winter
D000682:Amyloid / Q000737:chemistry*; D001703:Biophysics / Q000379:methods*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007328:Insulin / Q000737:chemistry / Q000378:metabolism*; D015233:Models, Statistical; D008962:Models, Theoretical; D009113:Muramidase / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D011336:Probability; D011485:Protein Binding; D011489:Protein Denaturation; D012542:Scattering, Radiation; D055672:Static Electricity; D013696:Temperature
D000682:Amyloid; D007328:Insulin; D010455:Peptides; D009113:Muramidase