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Your search keyword '"Zhengya Gao"' showing total 3 results
Start Over Author "Zhengya Gao" Publisher elsevier bv
3 results on '"Zhengya Gao"'

1. Deuteration of the farnesyl terminal methyl groups of δ-tocotrienol and its effects on the metabolic stability and ability of inducing G-CSF production

Author

Peter A. Crooks, Daohong Zhou, Zhengya Gao, Peiyi Zhang, Xuan Zhang, Howard P. Hendrickson, Lin Song, Xingui Liu, Qiang Fu, and Guangrong Zheng

Subjects
Male, Metabolite, medicine.medical_treatment, Clinical Biochemistry, Pharmaceutical Science, Radiation-Protective Agents, 01 natural sciences, Biochemistry, Article, Mice, Structure-Activity Relationship, chemistry.chemical_compound, Pharmacokinetics, In vivo, Granulocyte Colony-Stimulating Factor, Drug Discovery, medicine, Animals, Vitamin E, Potency, Molecular Biology, Dose-Response Relationship, Drug, Molecular Structure, 010405 organic chemistry, Organic Chemistry, In vitro, 0104 chemical sciences, Bioavailability, 010404 medicinal & biomolecular chemistry, chemistry, Molecular Medicine, Tocotrienol
Abstract

δ-tocotrienol (DT3), a member of vitamin E family, has been shown to have potent radio-protective effect. However, its application as a radioprotectant has limited, at least in part, by its short plasma elimination half-life and low bioavailability. In an effort to increase the metabolic stability of DT3, a deuterium substituted DT3 derivative, d(6)-DT3, was designed and synthesized. d(6)-DT3 showed improved in vitro and in vivo metabolic stability compared to DT3. The unexpected lower potency of d(6)-DT3 in inducing granulocyte-colony stimulating factor (G-CSF) production in mouse revealed that the metabolite(s) of DT3 might play a major role in inducing G-CSF induction.

Published
2020

2. Calcium-induced changes in calmodulin structural dynamics and thermodynamics

Author

Aichun Dong, Guangrong Wu, Shaoning Yu, and Zhengya Gao

Subjects
Models, Molecular, Conformational change, Calmodulin, Protein Conformation, Thermodynamics, Cooperativity, Plasma protein binding, Biochemistry, Substrate Specificity, Structural Biology, Denaturation (biochemistry), Fourier transform infrared spectroscopy, Binding site, Molecular Biology, Guanidine, Protein Unfolding, Binding Sites, biology, Protein Stability, Chemistry, Spectrum Analysis, Water, Isothermal titration calorimetry, General Medicine, Crystallography, biology.protein, Calcium, Protein Binding
Abstract

The thermodynamics of the interaction between Ca(2+) and calmodulin (CaM) was examined using isothermal titration calorimetry (ITC). The chemical denaturation of calmodulin was monitored spectroscopically to determine the stability of Ca(2+)-free (apo) and Ca(2+)-loaded (holo) CaMs. We explored the conformational and structural dynamics of CaM using amide hydrogen-deuterium (H-D) exchange coupled with Fourier transform infrared (FT-IR) spectroscopy. The results of H-D exchange and FT-IR suggest that CaM activation by Ca(2+) binding involves significant conformational changes. The results have also revealed that while the overall conformation of holo-CaM is more stable than that of the apo-CaM, some part of its α-helix structures, most likely the EF-hand domain region, has more solvent exposure, thus, has a faster H-D exchange rate than that of the apo-CaM. The ITC method provides a new strategy for obtaining site-specific Ca(2+) binding properties and a better estimation of the cooperativity and conformational change contributions of coupled EF-hand proteins.

Published
2012

3. Roles of hinge region, loops 3 and 4 in the activation of Escherichia coli cyclic AMP receptor protein

Author

Ting Yu, Guangrong Wu, Zhengya Gao, Feng Li, Shaoning Yu, and Yanrun Zhu

Subjects
Conformational change, Cyclic AMP Receptor Protein, Macromolecular Substances, Protein Conformation, Amino Acid Motifs, Allosteric regulation, lac operon, Calorimetry, medicine.disease_cause, Biochemistry, Structural Biology, Escherichia coli, medicine, Chymotrypsin, Molecular Biology, biology, Chemistry, Circular Dichroism, Escherichia coli Proteins, Temperature, General Medicine, Protein Structure, Tertiary, Cell biology, Kinetics, Spectrometry, Fluorescence, cAMP receptor protein, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, biology.protein, CAMP binding, CREB1, Dimerization, Protein Binding, Signal Transduction
Abstract

The cAMP receptor protein (CRP) requires cAMP for an allosteric change and regulates more than 150 genes in Escherichia coli. In this study, the modular half of cAMP receptor protein was used to investigate the allosteric signal transmission pathway induced by cAMP binding. The activation of CRP upon cAMP binding is indicated to be realignment of the two subunits within the CRP dimer. The interaction of loop 3 and Phe136 do not involve in signal transmission.

Published
2012

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