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Related Concept Videos

Peptide Bonds02:43

Peptide Bonds

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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Metallic solids such as crystals of copper, aluminum, and iron are formed by metal atoms. The structure of metallic crystals is often described as a uniform distribution of atomic nuclei within a “sea” of delocalized electrons. The atoms within such a metallic solid are held together by a unique force known as metallic bonding that gives rise to many useful and varied bulk properties.
All metallic solids exhibit high thermal and electrical conductivity, metallic luster, and malleability....
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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
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The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
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Metallic bonds are formed between two metal atoms. A simplified model to describe metallic bonding has been developed by Paul Drüde called the “Electron Sea Model”. 
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Synthesis and Characterization of Functionalized Metal-organic Frameworks
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Sequence-Dependent Peptide Surface Functionalization of Metal-Organic Frameworks.

Gang Fan, Christopher M Dundas, Cheng Zhang

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    |May 16, 2018
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    Summary
    This summary is machine-generated.

    Researchers developed a method to attach peptides to metal-organic frameworks (MOFs) using phage display. This peptide functionalization enhances MOF stability, controlling drug release in aqueous environments.

    Keywords:
    metal−organic frameworkspeptidesphage display and drug deliverysurface functionalization

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    Area of Science:

    • Materials Science
    • Biotechnology
    • Nanotechnology

    Background:

    • Metal-organic frameworks (MOFs) are porous materials with diverse applications.
    • Water stability and controlled functionalization are key challenges for MOF applications.
    • Peptide functionalization offers a route to modify MOF properties.

    Purpose of the Study:

    • To develop a noncovalent surface functionalization technique for water-stable MOFs using peptides.
    • To identify and characterize peptides that bind specifically to different MOF structures.
    • To investigate the impact of peptide functionalization on MOF stability and drug release kinetics.

    Main Methods:

    • Phage display for identifying MOF-specific peptides.
    • Thermodynamic binding affinity and specificity measurements.
    • Electron microscopy, powder X-ray diffraction, and gas adsorption for material characterization.
    • Confocal laser-scanning microscopy and surface area measurements for localization and pore accessibility.
    • pH-dependent drug release studies using fluorescein.

    Main Results:

    • Specific peptides were identified for crystalline ZIF-8, semiamorphous Fe-BTC, and MIL-53(Al)-FA MOFs.
    • Peptide functionalization did not alter MOF characteristics (morphology, crystallinity, porosity).
    • Peptides were localized on the MOF surface without pore blockage.
    • Peptide binding improved MOF stability at low pH, attenuating fluorescein release.

    Conclusions:

    • Phage display is a versatile method for discovering peptides with high affinity for water-stable MOFs.
    • Peptide functionalization can enhance MOF stability in aqueous environments.
    • This approach offers a strategy to modulate drug release kinetics by controlling MOF stability.