MyMedR

Displaying all 4 publications

Abstract:

Sort:

Microwave assisted synthesis of 2,2'-arylene-substituted bis(4H-3,1-benzoxazin-4-one) derivatives using the complex cyanuric chloride/N,N-dimethylformamide

Shariat M, Samsudin MW, Zakaria Z

Molecules, 2012 Sep 28;17(10):11607-15.
PMID: 23023686

A new and efficient method has been designed to prepare 2,2'-arylene-substituted bis(4H-3,1-benzoxazin-4-one) derivatives by using the mixture of cyanuric chloride and N,N-dimethylformamide in a microwave-assisted reaction. The method used and presented here has good rate enhancement and excellent yields.

Matched MeSH terms: ortho-Aminobenzoates/chemistry
Exploring the interaction between the antiallergic drug, tranilast and human serum albumin: Insights from calorimetric, spectroscopic and modeling studies

Tayyab S, Zaroog MS, Feroz SR, Mohamad SB, Malek SN

Int J Pharm, 2015 Aug 1;491(1-2):352-8.
PMID: 26142245 DOI: 10.1016/j.ijpharm.2015.06.042

The interaction of tranilast (TRN), an antiallergic drug with the main drug transporter in human circulation, human serum albumin (HSA) was studied using isothermal titration calorimetry (ITC), fluorescence spectroscopy and in silico docking methods. ITC data revealed the binding constant and stoichiometry of binding as (3.21 ± 0.23) × 10(6)M(-1) and 0.80 ± 0.08, respectively, at 25°C. The values of the standard enthalpy change (ΔH°) and the standard entropy change (ΔS°) for the interaction were found as -25.2 ± 5.1 kJ mol(-1) and 46.9 ± 5.4 J mol(-1)K(-1), respectively. Both thermodynamic data and modeling results suggested the involvement of hydrogen bonding, hydrophobic and van der Waals forces in the complex formation. Three-dimensional fluorescence data of TRN-HSA complex demonstrated significant changes in the microenvironment around the protein fluorophores upon drug binding. Competitive drug displacement results as well as modeling data concluded the preferred binding site of TRN as Sudlow's site I on HSA.

Matched MeSH terms: ortho-Aminobenzoates/chemistry*
Efficient Synthesis and Discovery of Schiff Bases as Potent Cholinesterase Inhibitors

Razik BM, Osman H, Ezzat MO, Basiri A, Salhin A, Kia Y, et al.

Med Chem, 2016;12(6):527-36.
PMID: 26833077

BACKGROUND: The search for new cholinesterase inhibitors is still a promising approach for management of Alzheimer`s disease. Schiff bases are considered as important class of organic compounds, which have wide range of applications including as enzyme inhibitors. In the present study, a new green ionic liquid mediated strategy was developed for convenient synthesis of two series of Schiff bases 3(a-j) and 5(a-j) as potential cholinesterase inhibitors using aromatic aldehydes and primary amines in [bmim]Br.
METHODS: The synthesized compounds were evaluated for their acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibitory potential by modified Ellman's method. The molecular interactions between the most active compound and the enzyme were analyzed by molecular docking.
RESULTS: Among them, 3j displayed higher inhibitory activities than reference drug, galanthamine, with IC50 values of 2.05 and 5.77 µM, for AChE and BChE, respectively. Interestingly, all the compounds except 3b displayed higher BChE inhibitions than galanthamine with IC50 values ranging from 5.77 to 18.52 µM. Molecular docking of compound 3j inside the TcAChE and hBChE completely coincided with the inhibitory activities observed. The compound forms strong hydrogen bonding at the peripheral anionic site of AChE whereas on BChE, it had hydrophobic and mild polar interactions.
CONCLUSION: An efficient and eco-friendly synthetic methodology has been developed to synthesize Schiff bases in a very short reaction time and excellent yields in ionic solvent, whereby the compounds from series 3 showed promising cholinesterase inhibitory activity.

Matched MeSH terms: para-Aminobenzoates/chemistry*
Opantimycin A, a new metabolite isolated from Streptomyces sp. RK88-1355

Nogawa T, Okano A, Lim CL, Futamura Y, Shimizu T, Takahashi S, et al.

J Antibiot (Tokyo), 2017 02;70(2):222-225.
PMID: 27599762 DOI: 10.1038/ja.2016.113
Matched MeSH terms: Aminobenzoates/chemistry*