Induced long-range attractive potentials of human serum albumin by ligand binding.
Small-angle x-ray scattering and dielectric spectroscopy investigation on the solutions of recombinant human serum albumin and its heme hybrid revealed that heme incorporation induces a specific long-range attractive potential between protein molecules. This is evidenced by the enhanced forward intensity upon heme binding, despite no hindrance to rotatory Brownian motion, unbiased colloid osmotic pressure, and discontiguous nearest-neighbor distance, confirming monodispersity of the proteins. The heme-induced potential may play a trigger role in recognition of the ligand-filled human serum albumins in the circulatory system.
Sato
Takaaki
T
Division of Pure and Applied Physics, Faculty of Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Japan. takaaki.sato@waseda.jp
Komatsu
Teruyuki
T
Nakagawa
Akito
A
Tsuchida
Eishun
E
D006418:Heme / Q000737:chemistry*; D006801:Humans; D011994:Recombinant Proteins / Q000737:chemistry; D012542:Scattering, Radiation; D012709:Serum Albumin / Q000737:chemistry*; D013057:Spectrum Analysis / Q000379:methods; D055672:Static Electricity; D014961:X-Ray Diffraction / Q000379:methods
D011994:Recombinant Proteins; D012709:Serum Albumin; D006418:Heme