Abstract
Providing fundamental information on intra/intermolecular interactions and physicochemical properties, the three-dimensional structural characterization of biological macromolecules is of extreme importance towards understanding their mechanism of action. Among other methods, X-ray powder diffraction (XRPD) has proved its applicability and efficiency in numerous studies of different materials. Owing to recent methodological advances, this method is now considered a respectable tool for identifying macromolecular phase transitions, quantitative analysis, and determining structural modifications of samples ranging from small organics to full-length proteins. An overview of the XRPD applications and recent improvements related to the study of challenging macromolecules and peptides toward structure-based drug design is discussed. This review congregates recent studies in the field of drug formulation and delivery processes, as well as in polymorph identification and the effect of ligands and environmental conditions upon crystal characteristics. These studies further manifest the efficiency of protein XRPD for quick and accurate preliminary structural characterization.
Highlights
X-ray crystallography has been for more than sixty years the most accurate and reliable approach to obtain detailed structural information for biological macromolecules
Has been considered the most powerful structural characterization tool for proteins, limitations related to the requirement of a sizeable single-crystal, stability, and diffraction quality have considerably reduced the number of molecules that can be studied via this method [3]
XRPDphase is a front-line in polymorph screening, as it provides a fingerprint of every between the various crystalline forms can be observed by examining the peak positions and crystalline phase exhibiting a unique diffraction pattern
Summary
X-ray crystallography has been for more than sixty years the most accurate and reliable approach to obtain detailed structural information for biological macromolecules. A steadily increasing number of studies has underlined efficiency of the powder diffraction method in a wide spectrum of fields, including structure determination of zeolites, small organic molecules [8,17,18,19], and, more recently, biological macromolecules [9,20,21,22,23,24,25,26,27]. XRPD is extensively used for the identification of specific components when examining intermixtures of inorganics or small organics, while its applicability is steadily increasing in the context of characterizing new pharmaceutically important phases of biological macromolecules which, in combination with the crystalline nature of the corresponding compound, may display advantageous properties as increased solubility and prolonged release of the beneficial agent [24,34]. The experimental results presented confirm the suitability of the method for both the extraction of structural information and polymorph screening for the purpose of therapeutics’ amelioration and design
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