J. T. Kilembe, Albert S. Lundemba, Dikima D. Bibelayi, Glodi M. Ndefi, Juliette Pradon, Zéphyrin G. Yav
The interference of human heat shock protein 90 (HSP90) in many signalling networks associated with cancer progression makes it an important drug target. In the present work, we investigated the binding ability of 9 selenoderivatives of geldanamycin (GMDSe) at the N-terminal domain of HSP90 derived from Protein Data Bank (PDB code: 1YET) based on ligand-protein docking. All selenoderivatives interacted positively with HSP90, yet the binding strength decreased when replacing monovalent oxygen in position 1 (GMDSe1) or 9 (GMDSe9). Hydrogen-bonding and lipophilic interactions between selenoderivatives and amino acid residues in the inhibitor site of HSP90 were thermodynamically the main forces driving the binding stability. Molecular electrostatic potential surfaces of the selenoderivatives showed marked non polar areas, which were probably involved in the lipophilic interactions with the hydrophobic residues of amino acids. Interestingly, the amino acid residues forming the hydrogen bonds with GMD were also involved in the hydrogen-bonding interactions with the selenoderivatives. Moreover, HSP90 interacted with the GMDSe6 and GMDSe7 selenoderivatives stronger than with GMD, while maintaining lipophilic interactions and hydrogen bonds with amino acid residues like Asp93, which are catalytically crucial for therapeutic properties of HSP90 inhibitors. This finding should guide further studies of pharmacophore properties of GMD selenoderivatives in order to explore their therapeutic properties. It is noteworthy that selenium has been suggested to reduce the risk of various types of cancers.
{"title":"Docking of Human Heat Shock Protein 90 with Selenoderivatives of Geldanamycin","authors":"J. T. Kilembe, Albert S. Lundemba, Dikima D. Bibelayi, Glodi M. Ndefi, Juliette Pradon, Zéphyrin G. Yav","doi":"10.4236/csta.2019.82002","DOIUrl":"https://doi.org/10.4236/csta.2019.82002","url":null,"abstract":"The interference of human heat shock protein 90 (HSP90) in many signalling networks associated with cancer progression makes it an important drug target. In the present work, we investigated the binding ability of 9 selenoderivatives of geldanamycin (GMDSe) at the N-terminal domain of HSP90 derived from Protein Data Bank (PDB code: 1YET) based on ligand-protein docking. All selenoderivatives interacted positively with HSP90, yet the binding strength decreased when replacing monovalent oxygen in position 1 (GMDSe1) or 9 (GMDSe9). Hydrogen-bonding and lipophilic interactions between selenoderivatives and amino acid residues in the inhibitor site of HSP90 were thermodynamically the main forces driving the binding stability. Molecular electrostatic potential surfaces of the selenoderivatives showed marked non polar areas, which were probably involved in the lipophilic interactions with the hydrophobic residues of amino acids. Interestingly, the amino acid residues forming the hydrogen bonds with GMD were also involved in the hydrogen-bonding interactions with the selenoderivatives. Moreover, HSP90 interacted with the GMDSe6 and GMDSe7 selenoderivatives stronger than with GMD, while maintaining lipophilic interactions and hydrogen bonds with amino acid residues like Asp93, which are catalytically crucial for therapeutic properties of HSP90 inhibitors. This finding should guide further studies of pharmacophore properties of GMD selenoderivatives in order to explore their therapeutic properties. It is noteworthy that selenium has been suggested to reduce the risk of various types of cancers.","PeriodicalId":67661,"journal":{"name":"晶体结构理论与应用(英文)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2019-05-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42760374","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
A new decavanadate, (C4N2H7)4(C6N2H10)V10O28·2H2O, was synthesized by slow evaporation at room temperature and characterized by single crystal X-ray diffraction, IR and UV-Vis spectroscopies. The compound crystallizes in the triclinic system, P-1 space group with the cell parameters: a = 11.200(5) A, b = 12.056(9) A, c =20.511(7) A, α = 73.40(4), β = 84.67(3), γ = 63.51(5), Z = 2 and volume V = 2373.7(1) A3. The formula unit is composed of one decavanadate [V10O28]6- anion, four 2-methylimidazolium (C4N2H7)+ cations, one 2-amino-4-picolinium (C6N2H10)2+ cation and two water molecules. In the crystal, the layers of decavanadate groups, organic cations and water molecules stack up parallel to the (011) plane. The cohesion is provided by N-H···O, O-H···O hydrogen bonds and Van der Waals interactions leads to a three-dimensional structure. The absorbance spectrum measurement shows an optical band gap of 3.27 eV which allows us to conclude that this compound is a semiconductor material.
采用室温慢蒸发法制备了一种新型十氰酸盐(C4N2H7)4(C6N2H10)V10O28·2H2O，并用单晶x射线衍射、红外光谱和紫外可见光谱对其进行了表征。晶胞参数为:a = 11.200(5) a, b = 12.056(9) a, c =20.511(7) a， α = 73.40(4)， β = 84.67(3)， γ = 63.51(5)， Z =2，体积V = 2373.7(1) A3。该配方单元由1个十氰酸盐[V10O28]6-阴离子、4个2-甲基咪唑(C4N2H7)+阳离子、1个2-氨基-4-吡啶(C6N2H10)2+阳离子和2个水分子组成。在晶体中，十氰酸盐基团、有机阳离子和水分子层与(011)平面平行堆叠。内聚力由N-H··O、O- h··O氢键提供，范德华相互作用形成三维结构。吸收光谱测量显示该化合物的光学带隙为3.27 eV，这使我们可以得出结论，该化合物是半导体材料。
{"title":"Preparation, Crystal Structure and Spectroscopy Characterization of Vanadium(V) Complex, 2-Amino-4-Picolinium, 2-Methylimidazolium Decavanadate Hydrate (C4N2H7)4(C6N2H10)V10O28·2H2O","authors":"Myriam Louati, R. Ksiksi, L. Jouffret, M. Zid","doi":"10.4236/csta.2019.81001","DOIUrl":"https://doi.org/10.4236/csta.2019.81001","url":null,"abstract":"A new decavanadate, (C4N2H7)4(C6N2H10)V10O28·2H2O, was synthesized by slow evaporation at room temperature and characterized by single crystal X-ray diffraction, IR and UV-Vis spectroscopies. The compound crystallizes in the triclinic system, P-1 space group with the cell parameters: a = 11.200(5) A, b = 12.056(9) A, c =20.511(7) A, α = 73.40(4), β = 84.67(3), γ = 63.51(5), Z = 2 and volume V = 2373.7(1) A3. The formula unit is composed of one decavanadate [V10O28]6- anion, four 2-methylimidazolium (C4N2H7)+ cations, one 2-amino-4-picolinium (C6N2H10)2+ cation and two water molecules. In the crystal, the layers of decavanadate groups, organic cations and water molecules stack up parallel to the (011) plane. The cohesion is provided by N-H···O, O-H···O hydrogen bonds and Van der Waals interactions leads to a three-dimensional structure. The absorbance spectrum measurement shows an optical band gap of 3.27 eV which allows us to conclude that this compound is a semiconductor material.","PeriodicalId":67661,"journal":{"name":"晶体结构理论与应用(英文)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2019-02-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45361316","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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