Interaction of anti-aggregation agent dimethylethylammonium propane sulfonate with acidic fibroblast growth factor.
Prevention of aggregation is critical for analyzing protein structure. Non-detergent sulfobetaines (NDSBs) are known to prevent protein aggregation, but the molecular mechanisms of their anti-aggregation effect are poorly understood. To elucidate the underlying mechanisms, we analyzed the effects of dimethylethylammonium propane sulfonate (NDSB-195) on acidic fibroblast growth factor (aFGF). NDSB-195 (0.5M) increased both aggregation and denaturation temperatures of aFGF by 4 degrees C. Chemical shift perturbation analyses indicated that many affected residues were located at the junction between a beta-strand (or 3(10)-helix) and a loop, irrespective of the chemical properties of the residue. The apparent dissociation constants of the interaction ranged from 0.04 to 3M, indicating weak interactions between NDSB and protein molecules.
Xiang
Long
L
Department of Chemistry and Chemical Biology, Graduate School of Engineering, Gunma University, 1-5-1 Tenjin-cho, Kiryu, Gunma 376-8515, Japan.
Ishii
Takeshi
T
Hosoda
Kazuo
K
Kamiya
Ayumi
A
Enomoto
Mayu
M
Nameki
Nobukazu
N
Inoue
Yusuke
Y
Kubota
Kenji
K
Kohno
Toshiyuki
T
Wakamatsu
Kaori
K
D001622:Betaine / Q000031:analogs & derivatives* / Q000737:chemistry; D019281:Dimerization; D016220:Fibroblast Growth Factor 1 / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D010975:Platelet Aggregation Inhibitors / Q000737:chemistry*; D011485:Protein Binding; D011489:Protein Denaturation; D025941:Protein Interaction Mapping / Q000379:methods*
C111794:NDSB 195; D010975:Platelet Aggregation Inhibitors; D016220:Fibroblast Growth Factor 1; D001622:Betaine