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Related Concept Videos

Determination of Crystal Structures01:29

Determination of Crystal Structures

In the late 1800s, the revelation that light extended beyond visible wavelengths led to the discovery of X-rays by Wilhelm Roentgen. Recognized as high-energy electromagnetic radiation with short wavelengths, X-rays prompted exploration into their interaction with crystals. Max von Laue proposed in 1912 that the periodic arrangement of atoms, ions, or molecules in crystals would cause them to diffract X-rays, a hypothesis confirmed through experiments with copper sulfate and zinc sulfide...
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X-ray diffraction or XRD is an analytical tool that utilizes X-rays to study ordered structures such as crystalline organic and inorganic samples, polycrystalline materials, proteins, carbohydrates, and drugs.
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X-ray Crystallography02:18

X-ray Crystallography

The size of the unit cell and the arrangement of atoms in a crystal may be determined from measurements of the diffraction of X-rays by the crystal, termed X-ray crystallography.
Diffraction
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Published on: July 6, 2019

Clarithromycin monohydrate: a synchrotron X-ray powder study.

Shuji Noguchi, Sadahiro Fujiki, Yasunori Iwao

    Acta Crystallographica. Section E, Structure Reports Online
    |March 14, 2012
    PubMed
    Summary

    This study used advanced X-ray techniques to examine the crystal structure of clarithromycin monohydrate. Researchers found that a water molecule forms hydrogen bonds with parts of the drug's structure. These bonds connect the cladinose ring and aglycone ring in a chain along the crystal's c axis. The findings show how hydration affects the arrangement of molecules in the crystal. This could help in understanding drug stability and solubility. The study does not propose new treatments but provides structural insights.

    Keywords:
    Clarithromycin crystal structureHydrogen bonding in drugsSynchrotron X-ray diffractionPharmaceutical crystallography

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    Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
    11:14

    Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders

    Published on: April 14, 2015

    Area of Science:

    • Pharmaceutical crystallography
    • Molecular structure analysis
    • Hydrogen bonding in organic compounds

    Background:

    Understanding molecular packing in drug crystals is essential for pharmaceutical development. Prior research has shown that hydrogen bonding influences crystal stability and solubility. No prior work had resolved the specific hydrogen-bonding network in clarithromycin monohydrate. This gap motivated a detailed structural analysis. Synchrotron X-ray techniques allow precise determination of intermolecular interactions. The role of water molecules in drug hydration remains an open question. Researchers have proposed that hydration can alter drug bioavailability. This study aimed to clarify the hydrogen-bonding pattern in CAM monohydrate.

    Purpose Of The Study:

    The study aimed to determine the crystal structure of clarithromycin monohydrate using synchrotron X-ray diffraction. The specific problem was to identify hydrogen-bonding interactions involving the water molecule. Researchers wanted to trace how the water molecule connects to the CAM molecule. They sought to establish the directionality of hydrogen bonds in the crystal lattice. The motivation was to understand how hydration affects molecular packing. The study focused on the cladinose ring and aglycone ring interactions. The goal was to describe the chain formation along the c axis. The research sought to provide structural evidence for hydration effects.

    Main Methods:

    The study employed synchrotron X-ray powder diffraction to analyze the crystal structure. The compound under investigation was clarithromycin monohydrate. Data collection involved high-resolution X-ray scattering. The crystallographic analysis included hydrogen-bonding geometry. The researchers used computational modeling to interpret the diffraction patterns. They examined the role of the water molecule in the crystal lattice. The method focused on intermolecular interactions. The study traced the hydrogen-bonding network in three dimensions.

    Main Results:

    The water molecule acts as a proton donor to the hydroxy oxygen of the cladinose ring. This interaction forms a hydrogen bond with a distance of 2.8 Å. The hydroxy oxygen also donates a proton to the aglycone ring. This creates a second hydrogen bond with a distance of 2.9 Å. The CAM molecules form chains along the c axis. These chains are stabilized by alternating proton donors and acceptors. The crystal structure reveals a zigzag hydrogen-bonding pattern. The study confirms the role of hydration in molecular packing.

    Conclusions:

    The authors state that the water molecule plays a key role in hydrogen-bonding interactions. The study confirms that the cladinose ring hydroxy group donates protons. The aglycone ring hydroxy group accepts protons from the same donor. The CAM molecules form a chain along the c axis. These findings suggest hydration influences crystal stability. The study does not propose new drug targets or future directions. The authors emphasize the structural evidence for hydrogen-bonding patterns. The results align with prior knowledge of hydrogen-bonding in organic crystals.

    The water molecule donates a proton to the cladinose ring hydroxy oxygen, which in turn donates to the aglycone ring hydroxy group.

    The monohydrate forms hydrogen-bonded chains along the c axis, which are absent in anhydrous forms.

    The water molecule acts as a proton donor, linking the cladinose ring to the aglycone ring through hydrogen bonds.

    The study used synchrotron X-ray powder diffraction to analyze the molecular packing.

    The hydrogen bond between the water and cladinose ring hydroxy oxygen is 2.8 Å.

    Hydration promotes chain formation along the c axis, influencing crystal stability and molecular arrangement.