scholarly journals Novel drug–drug cocrystals of carbamazepine with para-aminosalicylic acid: screening, crystal structures and comparative study of carbamazepine cocrystal formation thermodynamics

CrystEngComm ◽  
2017 ◽  
Vol 19 (30) ◽  
pp. 4273-4286 ◽  
Author(s):  
Ksenia V. Drozd ◽  
Alex N. Manin ◽  
Andrei V. Churakov ◽  
German L. Perlovich
Keyword(s):  
Comparative Study ◽  
Crystal Structures ◽  
Anticonvulsant Drug ◽  
Aminosalicylic Acid ◽  
Antituberculous Drug ◽  
Novel Drug ◽  
Formation Thermodynamics

The cocrystal formation of the anticonvulsant drug carbamazepine (CBZ) with para-aminosalicylic acid (PASA, antituberculous drug) has been studied by varying methods.

Saccharin salts of biologically active hydrazone derivatives

2015 ◽  
Vol 39 (11) ◽  
pp. 8614-8622 ◽  
Author(s):  
Artem O. Surov ◽  
Alexander P. Voronin ◽  
Anna A. Simagina ◽  
Andrei V. Churakov ◽  
Sophia Y. Skachilova ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Biologically Active ◽  
Formation Thermodynamics

Crystal structures, solubility and formation thermodynamics of saccharin salts with biologically active hydrazone derivatives were investigated.

scholarly journals Domain sliding of two Staphylococcus aureus N-acetylglucosaminidases enables their substrate-binding prior to its catalysis

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Sara Pintar ◽  
Jure Borišek ◽  
Aleksandra Usenik ◽  
Andrej Perdih ◽  
Dušan Turk
Keyword(s):  
Crystal Structures ◽  
Active Site ◽  
Drug Targets ◽  
Substrate Binding ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Human Pathogen ◽  
Active Site Cleft ◽  
Novel Drug ◽  
Novel Drug Targets

AbstractTo achieve productive binding, enzymes and substrates must align their geometries to complement each other along an entire substrate binding site, which may require enzyme flexibility. In pursuit of novel drug targets for the human pathogen S. aureus, we studied peptidoglycan N-acetylglucosaminidases, whose structures are composed of two domains forming a V-shaped active site cleft. Combined insights from crystal structures supported by site-directed mutagenesis, modeling, and molecular dynamics enabled us to elucidate the substrate binding mechanism of SagB and AtlA-gl. This mechanism requires domain sliding from the open form observed in their crystal structures, leading to polysaccharide substrate binding in the closed form, which can enzymatically process the bound substrate. We suggest that these two hydrolases must exhibit unusual extents of flexibility to cleave the rigid structure of a bacterial cell wall.

The Anion [Co(C8H12)2]–. A Comparative Study of the Crystal Structures of [{K(18-crown-6)}2(C5H5)][Co(C8H12)2] and Co(C8H12)(C8H13)

2009 ◽  
Vol 64 (8) ◽  
pp. 985-988 ◽  
Author(s):  
Jian-Qiang Wang ◽  
Thomas F. Fässler
Keyword(s):  
Crystal Structure ◽  
Crown Ether ◽  
Comparative Study ◽  
Single Crystal ◽  
Crystal Structures ◽  
Structure Determination ◽  
Cobalt Complex ◽  
Crystal Structure Determination ◽  
X Ray ◽  
Cyclopentadienyl Anion

The cobalt complex [{K(18-crown-6)}2(C5H5)]- [Co(C8H12)2]・(THF)2 (3) has been synthesized and characterized by X-ray single-crystal structure determination. The crystal structure of Co(C8H12)(C8H13) (2) has been reinvestigated and compared with the structure of 3. The 1,5-cyclooctadiene (C8H12) and C8H13 ligands are coordinated in an η4 and η3 fashion, respectively. The cyclopentadienyl anion in [{K(18-crown-6)}2(C5H5)]+ in 3 is η5-coordinated to the two crown ether-encapsulated potassium cations

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