Polydispersity as a Parameter for Indicating the Thermal Stability of Proteins by Dynamic Light Scattering

SHIBA Kohei, NIIDOME Takuro, KATOH Etsuko, XIANG Hongyu, HAN Lu, MORI Takeshi, KATAYAMA Yoshiki

doi:10.2116/analsci.26.659

Polydispersity as a Parameter for Indicating the Thermal Stability of Proteins by Dynamic Light Scattering

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SHIBA Kohei

Department of Applied Chemistry, Faculty of Engineering, Kyushu University Sysmex Corporation
NIIDOME Takuro

Department of Applied Chemistry, Faculty of Engineering, Kyushu University Center for Future Chemistry, Kyushu University PRESTO, Japan Science and Technology Corporation
KATOH Etsuko

Division of Plant Research, National Institute of Agrobiological Sciences
XIANG Hongyu

Division of Plant Research, National Institute of Agrobiological Sciences
HAN Lu

Division of Plant Research, National Institute of Agrobiological Sciences
MORI Takeshi

Department of Applied Chemistry, Faculty of Engineering, Kyushu University Center for Future Chemistry, Kyushu University
KATAYAMA Yoshiki

Department of Applied Chemistry, Faculty of Engineering, Kyushu University Center for Future Chemistry, Kyushu University

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説明

A physical parameter for predicting the thermal stability of proteins was provided by a new approach using dynamic light scattering (DLS). The relationship between the melting point measured by differential scanning calorimetry (DSC) and the polydispersity of the hydrodynamic diameter determined by DLS analysis was examined. Calmodulin (CaM) and concanavalin A (ConA) were used as model proteins. The melting point measured by DSC, an indicator for thermal stability, increased and the polydispersity decreased on binding of the proteins to specific ligands, suggesting that the polydispersity could be used an indicator to predict thermal stability. In addition, the increase of thermal stability that resulted from forming a complex could be quantified by polydispersity analysis even when the melting point changed only slightly.