Synchrotron X-Ray Powder Diffraction:‎ Crystal Structure Determination of New Phosphodiesterase Enzymes Inhibitor

Abstract

Single crystal X-ray diffraction analysis is the usual way in the determination of structure of crystalline solids. ‎Nowadays, however, many materials such as pharmaceutical compounds cannot be easily crystallized and exist ‎only as powders. In these cases powder diffraction arises as an alternative. Synchrotron radiation is the most ‎powerful source of X-rays currently available for powder diffraction experiments. Narrow peaks, accurate peak ‎positions and excellent signal to background ratios means that synchrotron data are ideal for structure solution ‎‎[1]. ‎<br><br><br><br>In this study, we focused on structure determination of 6-(4-(4-methylpiperazin-1-yl)-4-oxobutoxy)-4-‎methylquinolin-2(1H)-one as a phosphodiesterase (PDE) enzymes inhibitor which improve cardiac contractility ‎and may be used in congestive heart failure (CHF) which is a major cause of death in patients with heart disease ‎‎[2].‎