Specific features of supramolecular organisation and hydrogen bonding in proline cocrystals: a case study of fenamates and diclofenac

CrystEngComm ◽  
2018 ◽  
Vol 20 (43) ◽  
pp. 6970-6981 ◽  
Author(s):  
Artem O. Surov ◽  
Alexander P. Voronin ◽  
Mikhail V. Vener ◽  
Andrei V. Churakov ◽  
German L. Perlovich
Keyword(s):  
Hydrogen Bonding ◽  
Amino Acid ◽  
Naturally Occurring ◽  
Supramolecular Organisation

New zwitterionic cocrystals of fenamate drugs and diclofenac with the naturally occurring amino acid l-proline have been obtained and thoroughly characterised by a variety of experimental and theoretical techniques.

Functional Anticodon Architecture of Human tRNALys3Includes Disruption of Intraloop Hydrogen Bonding by the Naturally Occurring Amino Acid Modification, t6A†

Biochemistry ◽  
2000 ◽  
Vol 39 (44) ◽  
pp. 13396-13404 ◽  
Author(s):  
John W. Stuart ◽  
Zofia Gdaniec ◽  
Richard Guenther ◽  
Michal Marszalek ◽  
Elzbieta Sochacka ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Amino Acid ◽  
Acid Modification ◽  
Naturally Occurring ◽  
Amino Acid Modification

Enantioselective Nucleophilic Aromatic Substitution Reaction of Azlactones to Synthesize Quaternary α-Amino Acid Derivatives

Synlett ◽  
2020 ◽  
Author(s):  
Xiaohua Liu ◽  
Yi Li ◽  
Hao Pan ◽  
Wang-Yuren Li ◽  
Xiaoming Feng
Keyword(s):  
Hydrogen Bonding ◽  
Charge Transfer ◽  
Amino Acid ◽  
Substitution Reaction ◽  
Nucleophilic Aromatic Substitution ◽  
Amino Acid Derivatives ◽  
Amino Acid Esters ◽  
Aromatic Substitution ◽  
Charge Transfer Interaction ◽  
Acid Esters

AbstractAn asymmetric organocatalytic nucleophilic aromatic substitution reaction of azlactones with electron-deficient aryls was established. A variety of α-aryl α-alkyl α-amino acid esters and peptides were obtained in decent yields and stereoselectivities. A new bifunctional catalytic mode involving charge-transfer interaction and hydrogen bonding is proposed to explain the enantioselectivity.

The Hydrogen-Bonding Ability of the Amino Acid Glutamine Revealed by Neutron Diffraction Experiments

2012 ◽  
Vol 116 (45) ◽  
pp. 13308-13319 ◽  
Author(s):  
N. H. Rhys ◽  
A. K. Soper ◽  
L. Dougan
Keyword(s):  
Hydrogen Bonding ◽  
Amino Acid ◽  
Neutron Diffraction

CAN SEMIEMPIRICAL QUANTUM MODELS CALCULATE THE BINDING ENERGY OF HYDROGEN BONDING FOR BIOLOGICAL SYSTEMS?

2009 ◽  
Vol 08 (04) ◽  
pp. 691-711 ◽  
Author(s):  
FENG FENG ◽  
HUAN WANG ◽  
WEI-HAI FANG ◽  
JIAN-GUO YU
Keyword(s):  
Hydrogen Bonding ◽  
Amino Acid ◽  
Amino Acid Residue ◽  
Density Functional ◽  
Biological Systems ◽  
Binding Energies ◽  
Semiempirical Model ◽  
Hydrogen Bonded Systems ◽  
High Level ◽  
Hydrogen Bonded

A modified semiempirical model named RM1BH, which is based on RM1 parameterizations, is proposed to simulate varied biological hydrogen-bonded systems. The RM1BH is formulated by adding Gaussian functions to the core–core repulsion items in original RM1 formula to reproduce the binding energies of hydrogen bonding of experimental and high-level computational results. In the parameterizations of our new model, 35 base-pair dimers, 18 amino acid residue dimers, 14 dimers between a base and an amino acid residue, and 20 other multimers were included. The results performed with RM1BH were compared with experimental values and the benchmark density-functional (B3LYP/6-31G**/BSSE) and Möller–Plesset perturbation (MP2/6-31G**/BSSE) calculations on various biological hydrogen-bonded systems. It was demonstrated that RM1BH model outperforms the PM3 and RM1 models in the calculations of the binding energies of biological hydrogen-bonded systems by very close agreement with the values of both high-level calculations and experiments. These results provide insight into the ideas, methods, and views of semiempirical modifications to investigate the weak interactions of biological systems.

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