The Experts below are selected from a list of 24876 Experts worldwide ranked by ideXlab platform
Yang Meng - One of the best experts on this subject based on the ideXlab platform.
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disrupting the intramolecular interaction between proto oncogene c src sh3 domain and its self binding peptide ppii with rationally designed peptide ligands
Artificial Cells Nanomedicine and Biotechnology, 2018Co-Authors: Peng Zhou, Zhongyan Li, Heyi Wang, Zheng Chen, Yang MengAbstract:AbstractProto-oncogene non-receptor tyrosine protein kinase c-Src has been involved in the development, progression and metastasis of a variety of human cancers. This protein contains two self-binding peptide (SBP) sites separately between the SH3 domain and polyproline-II (PPII) helix and between the SH2 domain and C-terminal phosphorylatable tail (CTPT), which are potential targets of anticancer drugs to regulate the kinase activity. Here, we described an integrated protocol to systematically investigate the structural basis, energetic property and dynamics behaviour of PPII binding to SH3, and to rationally design potent peptide ligands to target the SBP site of SH3–PPII interaction. Our study found that the PPII peptide is a non-typical binder that can only interact effectively with its cognate SH3 domain when it is integrated into the full-length c-Src kinase protein; stripping the peptide from the protein would considerably impair SH3 affinity by Increasing Entropy penalty upon the domain–peptide bi...
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disrupting the intramolecular interaction between proto oncogene c src sh3 domain and its self binding peptide ppii with rationally designed peptide ligands
Artificial Cells Nanomedicine and Biotechnology, 2018Co-Authors: Peng Zhou, Heyi Wang, Zheng Chen, Shasha Hou, Zhengya Bai, Yang MengAbstract:Proto-oncogene non-receptor tyrosine protein kinase c-Src has been involved in the development, progression and metastasis of a variety of human cancers. This protein contains two self-binding peptide (SBP) sites separately between the SH3 domain and polyproline-II (PPII) helix and between the SH2 domain and C-terminal phosphorylatable tail (CTPT), which are potential targets of anticancer drugs to regulate the kinase activity. Here, we described an integrated protocol to systematically investigate the structural basis, energetic property and dynamics behaviour of PPII binding to SH3, and to rationally design potent peptide ligands to target the SBP site of SH3-PPII interaction. Our study found that the PPII peptide is a non-typical binder that can only interact effectively with its cognate SH3 domain when it is integrated into the full-length c-Src kinase protein; stripping the peptide from the protein would considerably impair SH3 affinity by Increasing Entropy penalty upon the domain-peptide binding, suggesting that the protein context plays an essential role in the SBP's biological function. Next, we identified that the PPII peptide binds to SH3 domain in a class II manner and, on this basis, we derived a series of modified versions of the wild-type PPII peptide using a structure-based rational strategy. These modified peptide mutants have been structurally optimized with respect to their molecular flexibility and interaction potency with SH3 domain, in order to minimize indirect Entropy penalty and to maximize direct binding enthalpy simultaneously. Consequently, several rationally designed peptides were obtained, including PPIIm2 (TSKPQTPGRA), PPIIm5 (KPPTPPRA), PPIIm6 (FPPPPPRA) and PPIIm7 (YPPLPPRA), which exhibit a moderately or considerably increased affinity (Kd = 72, 34, 15 and 5.7 μM, respectively) relative to the wild-type PPII (TSKPQTQGLA) (Kd = 160 μM). These peptides can be used as lead molecular entities to further develop new anticancer therapeutics to regulate c-Src kinase activity by targeting the SBP site of SH3-PPII interaction.
Uday Chand Ghosh - One of the best experts on this subject based on the ideXlab platform.
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manganese associated nanoparticles agglomerate of iron iii oxide synthesis characterization and arsenic iii sorption behavior with mechanism
Journal of Hazardous Materials, 2010Co-Authors: Kaushik Gupta, Arjun Maity, Uday Chand GhoshAbstract:Abstract Three samples of manganese associated hydrous iron(III) oxide (MNHFO), prepared by incinerating metal hydroxide precipitate at T (±5) = 90, 300 and 600 °C, showed increase of crystalline nature in XRD patterns with decreasing As(III) removal percentages. TEM images showed the increase of crystallinity from sample-1 (MNHFO-1) to sapmple-3 (MNHFO-3). Dimensions (nm) of particles estimated were 5.0, 7.0 and 97.5. Optimization of pH indicated that MNHFO-1 could remove aqueous As(III) efficiently at pH between 3.0 and 7.0. Kinetic and equilibrium data of reactions under the experimental conditions described the pseudo-second order and the Langmuir isotherm equations very well, respectively. The Langmuir capacity ( q m ) estimated was 691.04 mmol kg −1 . The values of enthalpy, Gibb's free energy and Entropy changes (Δ H 0 = +23.23 kJ mol −1 , Δ G 0 = −3.43 to −7.20 kJ mol −1 at T = 283–323 K, Δ S 0 = +0.094 kJ mol −1 K −1 ) suggested that the reaction was endothermic, spontaneous and took place with Increasing Entropy. The As(III) sorbed by MNHFO-1 underwent surface oxidation to As(V), and evidences appeared from the XPS and FTIR investigations. MNHFO-1 packed column (internal diameter: 1.0 cm, height: 3.7 cm) filtered 11.5 dm 3 groundwater (105 μg As dm −3 ) with reducing arsenic concentration to ≤10 μg dm −3 .
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arsenic removal using hydrous nanostructure iron iii titanium iv binary mixed oxide from aqueous solution
Journal of Hazardous Materials, 2009Co-Authors: Kaushik Gupta, Uday Chand GhoshAbstract:The synthetic bimetal iron(III)-titanium(IV) oxide (NHITO) used was characterized as hydrous and nanostructured mixed oxide, respectively, by the Fourier transform infra red (FTIR), X-ray diffraction (XRD) pattern and the transmission electron microscopic (TEM) image analyses. Removal of As(III) and As(V) using the NHITO was studied at pH 7.0 (+/-0.1) with variation of contact time, solute concentration and temperature. The kinetic sorption data, in general, for As(III) described the pseudo-first order while that for As(V) described the pseudo-second order equation. The Langmuir isotherm described the equilibrium data (303 (+/-1.6)K) of fit was well with the Langmuir model. The Langmuir capacity (q(m), mg g(-1)) value of the material is 85.0 (+/-4.0) and 14.0 (+/-0.5), respectively, for the reduced and oxidized species. The sorption reactions on NHITO were found to be endothermic and spontaneous, and took place with Increasing Entropy. The energy (kJ mol(-1)) of sorption for As(III) and As(V) estimated, respectively, is 9.09 (+/-0.01) and 13.51 (+/-0.04). The sorption percentage reduction of As(V) was significant while that of As(III) was insignificant in presence of phosphate and sulfate. The fixed bed NHITO column (5.1 cm x 1.0 cm) sorption tests gave 3.0, 0.7 and 4.5L treated water (As content < or = 0.01 mg L(-1)) from separate As(III) and As(V) spiked (0.35+/-0.02 mg L(-1)) natural water samples and from high arsenic (0.11+/-0.01 mg L(-1)) ground water, respectively when inflow rate was (0.06 L h(-1)).
Peng Zhou - One of the best experts on this subject based on the ideXlab platform.
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disrupting the intramolecular interaction between proto oncogene c src sh3 domain and its self binding peptide ppii with rationally designed peptide ligands
Artificial Cells Nanomedicine and Biotechnology, 2018Co-Authors: Peng Zhou, Zhongyan Li, Heyi Wang, Zheng Chen, Yang MengAbstract:AbstractProto-oncogene non-receptor tyrosine protein kinase c-Src has been involved in the development, progression and metastasis of a variety of human cancers. This protein contains two self-binding peptide (SBP) sites separately between the SH3 domain and polyproline-II (PPII) helix and between the SH2 domain and C-terminal phosphorylatable tail (CTPT), which are potential targets of anticancer drugs to regulate the kinase activity. Here, we described an integrated protocol to systematically investigate the structural basis, energetic property and dynamics behaviour of PPII binding to SH3, and to rationally design potent peptide ligands to target the SBP site of SH3–PPII interaction. Our study found that the PPII peptide is a non-typical binder that can only interact effectively with its cognate SH3 domain when it is integrated into the full-length c-Src kinase protein; stripping the peptide from the protein would considerably impair SH3 affinity by Increasing Entropy penalty upon the domain–peptide bi...
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disrupting the intramolecular interaction between proto oncogene c src sh3 domain and its self binding peptide ppii with rationally designed peptide ligands
Artificial Cells Nanomedicine and Biotechnology, 2018Co-Authors: Peng Zhou, Heyi Wang, Zheng Chen, Shasha Hou, Zhengya Bai, Yang MengAbstract:Proto-oncogene non-receptor tyrosine protein kinase c-Src has been involved in the development, progression and metastasis of a variety of human cancers. This protein contains two self-binding peptide (SBP) sites separately between the SH3 domain and polyproline-II (PPII) helix and between the SH2 domain and C-terminal phosphorylatable tail (CTPT), which are potential targets of anticancer drugs to regulate the kinase activity. Here, we described an integrated protocol to systematically investigate the structural basis, energetic property and dynamics behaviour of PPII binding to SH3, and to rationally design potent peptide ligands to target the SBP site of SH3-PPII interaction. Our study found that the PPII peptide is a non-typical binder that can only interact effectively with its cognate SH3 domain when it is integrated into the full-length c-Src kinase protein; stripping the peptide from the protein would considerably impair SH3 affinity by Increasing Entropy penalty upon the domain-peptide binding, suggesting that the protein context plays an essential role in the SBP's biological function. Next, we identified that the PPII peptide binds to SH3 domain in a class II manner and, on this basis, we derived a series of modified versions of the wild-type PPII peptide using a structure-based rational strategy. These modified peptide mutants have been structurally optimized with respect to their molecular flexibility and interaction potency with SH3 domain, in order to minimize indirect Entropy penalty and to maximize direct binding enthalpy simultaneously. Consequently, several rationally designed peptides were obtained, including PPIIm2 (TSKPQTPGRA), PPIIm5 (KPPTPPRA), PPIIm6 (FPPPPPRA) and PPIIm7 (YPPLPPRA), which exhibit a moderately or considerably increased affinity (Kd = 72, 34, 15 and 5.7 μM, respectively) relative to the wild-type PPII (TSKPQTQGLA) (Kd = 160 μM). These peptides can be used as lead molecular entities to further develop new anticancer therapeutics to regulate c-Src kinase activity by targeting the SBP site of SH3-PPII interaction.
Kaushik Gupta - One of the best experts on this subject based on the ideXlab platform.
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manganese associated nanoparticles agglomerate of iron iii oxide synthesis characterization and arsenic iii sorption behavior with mechanism
Journal of Hazardous Materials, 2010Co-Authors: Kaushik Gupta, Arjun Maity, Uday Chand GhoshAbstract:Abstract Three samples of manganese associated hydrous iron(III) oxide (MNHFO), prepared by incinerating metal hydroxide precipitate at T (±5) = 90, 300 and 600 °C, showed increase of crystalline nature in XRD patterns with decreasing As(III) removal percentages. TEM images showed the increase of crystallinity from sample-1 (MNHFO-1) to sapmple-3 (MNHFO-3). Dimensions (nm) of particles estimated were 5.0, 7.0 and 97.5. Optimization of pH indicated that MNHFO-1 could remove aqueous As(III) efficiently at pH between 3.0 and 7.0. Kinetic and equilibrium data of reactions under the experimental conditions described the pseudo-second order and the Langmuir isotherm equations very well, respectively. The Langmuir capacity ( q m ) estimated was 691.04 mmol kg −1 . The values of enthalpy, Gibb's free energy and Entropy changes (Δ H 0 = +23.23 kJ mol −1 , Δ G 0 = −3.43 to −7.20 kJ mol −1 at T = 283–323 K, Δ S 0 = +0.094 kJ mol −1 K −1 ) suggested that the reaction was endothermic, spontaneous and took place with Increasing Entropy. The As(III) sorbed by MNHFO-1 underwent surface oxidation to As(V), and evidences appeared from the XPS and FTIR investigations. MNHFO-1 packed column (internal diameter: 1.0 cm, height: 3.7 cm) filtered 11.5 dm 3 groundwater (105 μg As dm −3 ) with reducing arsenic concentration to ≤10 μg dm −3 .
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arsenic removal using hydrous nanostructure iron iii titanium iv binary mixed oxide from aqueous solution
Journal of Hazardous Materials, 2009Co-Authors: Kaushik Gupta, Uday Chand GhoshAbstract:The synthetic bimetal iron(III)-titanium(IV) oxide (NHITO) used was characterized as hydrous and nanostructured mixed oxide, respectively, by the Fourier transform infra red (FTIR), X-ray diffraction (XRD) pattern and the transmission electron microscopic (TEM) image analyses. Removal of As(III) and As(V) using the NHITO was studied at pH 7.0 (+/-0.1) with variation of contact time, solute concentration and temperature. The kinetic sorption data, in general, for As(III) described the pseudo-first order while that for As(V) described the pseudo-second order equation. The Langmuir isotherm described the equilibrium data (303 (+/-1.6)K) of fit was well with the Langmuir model. The Langmuir capacity (q(m), mg g(-1)) value of the material is 85.0 (+/-4.0) and 14.0 (+/-0.5), respectively, for the reduced and oxidized species. The sorption reactions on NHITO were found to be endothermic and spontaneous, and took place with Increasing Entropy. The energy (kJ mol(-1)) of sorption for As(III) and As(V) estimated, respectively, is 9.09 (+/-0.01) and 13.51 (+/-0.04). The sorption percentage reduction of As(V) was significant while that of As(III) was insignificant in presence of phosphate and sulfate. The fixed bed NHITO column (5.1 cm x 1.0 cm) sorption tests gave 3.0, 0.7 and 4.5L treated water (As content < or = 0.01 mg L(-1)) from separate As(III) and As(V) spiked (0.35+/-0.02 mg L(-1)) natural water samples and from high arsenic (0.11+/-0.01 mg L(-1)) ground water, respectively when inflow rate was (0.06 L h(-1)).
Zheng Chen - One of the best experts on this subject based on the ideXlab platform.
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disrupting the intramolecular interaction between proto oncogene c src sh3 domain and its self binding peptide ppii with rationally designed peptide ligands
Artificial Cells Nanomedicine and Biotechnology, 2018Co-Authors: Peng Zhou, Zhongyan Li, Heyi Wang, Zheng Chen, Yang MengAbstract:AbstractProto-oncogene non-receptor tyrosine protein kinase c-Src has been involved in the development, progression and metastasis of a variety of human cancers. This protein contains two self-binding peptide (SBP) sites separately between the SH3 domain and polyproline-II (PPII) helix and between the SH2 domain and C-terminal phosphorylatable tail (CTPT), which are potential targets of anticancer drugs to regulate the kinase activity. Here, we described an integrated protocol to systematically investigate the structural basis, energetic property and dynamics behaviour of PPII binding to SH3, and to rationally design potent peptide ligands to target the SBP site of SH3–PPII interaction. Our study found that the PPII peptide is a non-typical binder that can only interact effectively with its cognate SH3 domain when it is integrated into the full-length c-Src kinase protein; stripping the peptide from the protein would considerably impair SH3 affinity by Increasing Entropy penalty upon the domain–peptide bi...
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disrupting the intramolecular interaction between proto oncogene c src sh3 domain and its self binding peptide ppii with rationally designed peptide ligands
Artificial Cells Nanomedicine and Biotechnology, 2018Co-Authors: Peng Zhou, Heyi Wang, Zheng Chen, Shasha Hou, Zhengya Bai, Yang MengAbstract:Proto-oncogene non-receptor tyrosine protein kinase c-Src has been involved in the development, progression and metastasis of a variety of human cancers. This protein contains two self-binding peptide (SBP) sites separately between the SH3 domain and polyproline-II (PPII) helix and between the SH2 domain and C-terminal phosphorylatable tail (CTPT), which are potential targets of anticancer drugs to regulate the kinase activity. Here, we described an integrated protocol to systematically investigate the structural basis, energetic property and dynamics behaviour of PPII binding to SH3, and to rationally design potent peptide ligands to target the SBP site of SH3-PPII interaction. Our study found that the PPII peptide is a non-typical binder that can only interact effectively with its cognate SH3 domain when it is integrated into the full-length c-Src kinase protein; stripping the peptide from the protein would considerably impair SH3 affinity by Increasing Entropy penalty upon the domain-peptide binding, suggesting that the protein context plays an essential role in the SBP's biological function. Next, we identified that the PPII peptide binds to SH3 domain in a class II manner and, on this basis, we derived a series of modified versions of the wild-type PPII peptide using a structure-based rational strategy. These modified peptide mutants have been structurally optimized with respect to their molecular flexibility and interaction potency with SH3 domain, in order to minimize indirect Entropy penalty and to maximize direct binding enthalpy simultaneously. Consequently, several rationally designed peptides were obtained, including PPIIm2 (TSKPQTPGRA), PPIIm5 (KPPTPPRA), PPIIm6 (FPPPPPRA) and PPIIm7 (YPPLPPRA), which exhibit a moderately or considerably increased affinity (Kd = 72, 34, 15 and 5.7 μM, respectively) relative to the wild-type PPII (TSKPQTQGLA) (Kd = 160 μM). These peptides can be used as lead molecular entities to further develop new anticancer therapeutics to regulate c-Src kinase activity by targeting the SBP site of SH3-PPII interaction.
