Study of some physical properties and chemical kinetics for the interaction of albumin with amoxicillin and cephalexin

Other Title(s)

دراسة بعض الخواص الفيزيائية و الحركيات الكيميائية لارتباط الالبومين مع الاموكسسلين و السفالكسين

Dissertant

Habib, Ala Abd al-Zahrah

Thesis advisor

al-Rufai, Ilham M.

Comitee Members

al-Sadi, Khulud Abd Salih
al-Awwadi, Nagham Shakir Turki

University

University of Baghdad

Faculty

College of Science

Department

Chemistry Department

University Country

Iraq

Degree

Master

Degree Date

2011

English Abstract

Albumin is the most abundant protein in blood plasma, and due to its ligand binding properties, serves as a circulating depot for endogenous and exogenous (e.g.

drugs) compounds.

Antibiotics, a chemical substances produced by various specices of microorganisms that are capable to inhibit the growth or kills other microorganisms.

Many of them are widely used in the prevention and treatment of disease in humans and animals, and much information is available about their chemical and pharmacological effects.

In this work we tried to get information about the binding of some antibiotics (ampacilin and cephalexin) and albumin, and the influence of the solvent polarity and ionic strength on it.

The binding of amoxicillin and cephalexin to human serum albumin has been studied by UV-Vis.

Spectrophotometric measurements in phosphate buffer of pH 7.4 and three different temperature, 290, 300, 310K.

The UV absorption shows a change and a shift in the peales of the drugs and albumin, the two changes are indicative of complex formation.

The stiochiometry of the interaction were calculated by the method of continuous variations and it implied that the stiochiometric ratio of drug-albumin complexes at pH 7.4 is 1:1.

The equilibrium constants were calculated at three different temperatures (290, 300 and 310K), the obtained keq values were 4.2´105M for albumin-amoxicillin complex and 3.5´105M for albumincephalexin complex, their value increases with the increase in temperature.

The resulting thermodynamic function are presented in table 93-15), the negative value of free energy DG indicates a spontaneous interaction, and the positive value of enthalpy DH° and entropy DS° XVI showed that a hydrophobic interaction plays a role in the binding of albumin and drugs.

The kinetic studies of the interaction of the drugs with albumin follows the first order reaction equation, and a rate constant have value of 16´10-4 min-1 for amoxicillin-albumin interaction and 13.8´10-4 min-1 for cephalexin-albumin interaction.

In order to obtain a more information about the complexation of HAS and their drugs molecules the various thermodynamic functions were calculated as a function of ionic strength and polarity of solvent, the presence of alcohol and NaCl salt effected the value of Keq and the thermodynamic parameters.

Finally: The binding study of drugs with HAS is of great importance in understanding chemico-biological interaction for drug design.

Pharmacy, pharmacology and biochemistry.

This study is expected to provide important in sight into the interactions of the physiologically important protein HAS with an important drug used in various therapeutic regimes.

Main Subjects

Chemistry

Topics

• Proteins
• Chemical processes
• Chemical reactions
• Penicillin
• Albumins
• Amoxicillin

No. of Pages

146

Table of Contents

• APA
• MLA
• AMA

Language

English

Data Type

Arab Theses

Record ID

BIM-599951