Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 3 de 3
Filter
Add more filters










Database
Language
Publication year range
1.
Int J Biol Macromol ; 120(Pt A): 1232-1239, 2018 Dec.
Article in English | MEDLINE | ID: mdl-30171949

ABSTRACT

A manganese Schiff base complex with N,N'-1,2-phenylenediamine-bis(salicyladimine) was synthesized and characterized by X-ray crystallography. This complex was administered intragastrically to alloxan-diabetic mice 3 weeks. In vivo tests showed that the complex significantly lowered serum glucose levels in alloxan-diabetic mice at doses of 77 mg V kg-1. Meanwhile, this complex was investigated as dipeptidyl peptidase IV (DPP-IV) inhibitor for the treatment of type 2 diabetes. The compound exhibit moderate inhibition against DPP-IV and possessed an IC50 value of 30 µM. Lineweaver-Burk transformation of the inhibition kinetics data demonstrated that it was a noncompetitive inhibitor of DPP-IV and Ki value was 136.3 µM. Moreover, molecular modeling studies suggested that the complex could fit well within the active-site cleft of DPP-IV. An acute toxicity study showed that animals treated intragastically with complex 1 at a dose of 5.0 g/kg did not show any significantly abnormal signs. These preliminary results suggest that the manganese Schiff base complex can induce a hypoglycemic effect in alloxan-diabetic mice.


Subject(s)
Coordination Complexes/administration & dosage , Diabetes Mellitus, Type 2/drug therapy , Dipeptidyl-Peptidase IV Inhibitors/administration & dosage , Ethylenediamines/administration & dosage , Organometallic Compounds/administration & dosage , Animals , Blood Glucose/drug effects , Coordination Complexes/chemical synthesis , Coordination Complexes/chemistry , Diabetes Mellitus, Type 2/blood , Diabetes Mellitus, Type 2/pathology , Dipeptidyl Peptidase 4/chemistry , Dipeptidyl-Peptidase IV Inhibitors/chemical synthesis , Dipeptidyl-Peptidase IV Inhibitors/chemistry , Ethylenediamines/chemical synthesis , Ethylenediamines/chemistry , Glucose Tolerance Test , Humans , Mice , Mice, Inbred NOD , Molecular Docking Simulation , Organometallic Compounds/chemical synthesis , Organometallic Compounds/chemistry , Schiff Bases/chemistry
2.
J Inorg Biochem ; 175: 29-35, 2017 10.
Article in English | MEDLINE | ID: mdl-28692886

ABSTRACT

Two oxidovanadium(IV) complexes carrying Schiff base ligands obtained from the condensation of 4,5-dichlorobenzene-1,2-diamine and salicylaldehyde derivatives were synthesised and characterised, including their X-ray crystallographic structures. They were evaluated as dipeptidyl peptidase IV (DPP-IV) inhibitors for the treatment of type 2 diabetes. These compounds were moderate inhibitors of DPP-IV, with IC50 values of ca. 40µM. In vivo tests showed that complexes 1 and 2 could lower significantly the level of glucose in the blood of alloxan-diabetic mice at doses of 22.5mgV·kg-1 and 29.6mgV·kg-1, respectively. Moreover, molecular modeling studies suggested that the oxidovanadium complexes 1 and 2 could fit well into the active-site cleft of the kinase domain of DPP-IV. To the best of our knowledge, this is the first report of vanadium complexes capable of inhibiting DPP-IV.


Subject(s)
Coordination Complexes , Diabetes Mellitus, Experimental , Dipeptidyl Peptidase 4/chemistry , Dipeptidyl-Peptidase IV Inhibitors , Molecular Docking Simulation , Vanadium , Animals , Coordination Complexes/chemical synthesis , Coordination Complexes/chemistry , Coordination Complexes/pharmacology , Diabetes Mellitus, Experimental/drug therapy , Diabetes Mellitus, Experimental/enzymology , Dipeptidyl Peptidase 4/metabolism , Dipeptidyl-Peptidase IV Inhibitors/chemical synthesis , Dipeptidyl-Peptidase IV Inhibitors/chemistry , Dipeptidyl-Peptidase IV Inhibitors/pharmacology , Male , Mice , Mice, Inbred ICR , Protein Domains , Vanadium/chemistry , Vanadium/pharmacology
3.
Dalton Trans ; 41(47): 14397-403, 2012 Dec 21.
Article in English | MEDLINE | ID: mdl-23064659

ABSTRACT

Two novel bpy-bridged Co(II) Schiff base complexes have been synthesized by the hydro(solvo)thermal reactions of corresponding amino-acid-based Schiff bases, bpy and Co(NO(3))(2)·6H(2)O. The following formulae identify the two complexes: {[Co(napala)(bpy)(0.5)]·H(2)O}(n) (1) and [Co(napgly)(bpy)(0.5)](n) (2) [H(2)napala = N-(2-hydroxy-1-naphthylmethylidene)-D/L-alanine, H(2)napgly = N-(2-hydroxy-1-naphthylmethylidene)-glycine and bpy = 4,4'-bipyridine]. These two compounds have been characterized using single-crystal X-ray diffraction, infrared, powder X-ray diffraction, thermogravimetric analysis, optical spectra analysis, and magnetic measurement. Complex 1 features an unprecedented threefold interpenetrated diamond network based on the fan-shaped Co(II)(4)(µ(2)-napala)(4) molecular square node and bpy linker, which represents the first example of 3D framework among the amino-acid-based Schiff base complexes with salicylaldehyde or its derivatives. In 2, adjacent Co(II) ions are bridged by µ(2)-napgly(2-) to form left- and right-handed [Co(II)(µ(2)-napgly)](n) helical chains. These two types of helical chains are sustained alternately by a symmetrical bpy co-ligand into a 2D grid-based layer. The solid-state fluorescence of complexes 1 and 2 are quenched almost completely compared with free mixed-ligands at room temperature. Moreover, magnetic studies show the dominant antiferromagnetic coupling between the Co(II) centers mediated by the syn-anti-COO(-)-bridges in both complexes.


Subject(s)
Amino Acids/chemistry , Cobalt/chemistry , Pyridines/chemistry , Schiff Bases/chemistry , Crystallography, X-Ray , Models, Molecular , Molecular Conformation
SELECTION OF CITATIONS
SEARCH DETAIL
...