Galantamine-Curcumin Hybrids as Dual-Site Binding Acetylcholinesterase Inhibitors.

Galantamine (GAL) and curcumin (CU) are alkaloids used to improve symptomatically neurodegenerative conditions like Alzheimer's disease (AD). GAL acts mainly as an inhibitor of the enzyme acetylcholinesterase (AChE). CU binds to amyloid-beta (Aβ) oligomers and inhibits the formation of Aβ plaques.

Quantitative Structure - Pharmacokinetics Relationships for Plasma Protein Binding of Basic Drugs.

Purpose: Binding of drugs to plasma proteins is a common physiological occurrence which may have a profound effect on both pharmacokinetics and pharmacodynamics. The early prediction of plasma protein binding (PPB) of new drug candidates is an important step in drug development process. The present study is focused on the development of quantitative structure - pharmacokinetics relationship (QSPkR) for the negative logarithm of the free fraction of the drug in plasma (pfu) of basic drugs.

Quantitative Structure - Pharmacokinetic Relationships for Plasma Clearance of Basic Drugs with Consideration of the Major Elimination Pathway.

Purpose: The success of a new drug candidate is determined not only by its efficacy and safety, but also by proper pharmacokinetic behavior. The early prediction of pharmacokinetic parameters could save time and resources and accelerate drug development process. Plasma clearance (CL) is one of the key determinants of drug dosing regimen.

Quantitative Structure - Pharmacokinetics Relationships Analysis of Basic Drugs: Volume of Distribution.

Purpose: The early prediction of pharmacokinetic behavior is of paramount importance for saving time and resources and for increasing the success of new drug candidates. The steady-state volume of distribution (VDss) is one of the key pharmacokinetic parameters required for the design of a suitable dosage regimen. The aim of the study is to propose a quantitative structure - pharmacokinetics relationships (QSPkR) for VDss of basic drugs.

Studies on drug-human serum albumin binding: the current state of the matter.

Human serum albumin (HSA) is the major plasma protein with vital functions acting as depot and career for many endogenous (fatty acids, bilirubin, etc.) and exogenous substances (drugs, nutrients, etc.) in the blood.

Molecular basis of sulindac competition with specific markers for the major binding sites on human serum albumin.

This study deals with the competitive interactions of sulindac (CAS 38194-50-2) with specific markers for the major binding areas on human serum albumin (HSA): phenylbutazone (CAS 50-33-9) and warfarin (CAS 129-06-6) for Site I, and diazepam (CAS 439-14-5) for Site II. The method used is high-performance liquid affinity chromatography with HSA-immobilized stationary phase. The affinity constants during the cobinding are determined, and the major thermodynamic parameters are calculated.

Thermodynamic characterization of the binding process of sulindac to human serum albumin.

This study deals with the molecular basis of the binding of the anti-inflammatory drug sulindac (CAS 38194-50-2) to human serum albumin (HSA) using high-performance liquid affinity chromatography. The chromatography was carried out using a HSA-immobilized column and a predominantly aqueous mobile phase (67 mmol/l sodium phosphate buffer/propan-1-ol, 94:6 v/v). A small quantity of sulidac was injected onto the column while increasing concentrations of the same drug were added to the mobile phase.