Bioadsorption of proteins on large mesocage-shaped mesoporous alumina monoliths

Sherif A. El-Safty, M. A. Shenashen, M. Khairy

    Research output: Contribution to journalArticle

    23 Citations (Scopus)

    Abstract

    With the remarkable progress in the field of gene technology, proteins have gained an important function in the field of disease diagnosis and treatment. Protein bioadsorption has drawn increasing attention partly because of the promising advances for diagnostic assays, sensors, separations, and gene technology. Mesocage alumina has a cage-type structure with high surface area and pore volume, exhibiting superior capabilities for protein adsorption. In this study, we report the size-selective adsorption/removal of virtual proteins having different shapes, sizes, functions, and properties, including insulin, HopPmaL domain, lysozyme, galectin-3, β-lactoglobulin, α-1-antitrypsin, α-amylase, and myosin in aqueous water using mesocage alumina. The mesoporous alumina monoliths have unique morphology and physical properties and enhanced protein adsorption characteristics in terms of sample loading capacity and quantity, thereby ensuring a higher concentration of proteins, interior pore diffusivity, and encapsulation in a short period. Thermodynamic analysis shows that protein adsorption on mesocage alumina monoliths is favorable and spontaneous. Theoretical models have been studied to investigate the major driving forces to achieve the most optimal performance of protein adsorption. The development of ultra- or micrometer-scale morphology composed of mesocage-shaped mesoporous monoliths or alumina network clusters can be effectively used to encapsulate the macromolecules into the interior cage cavities, which can greatly assist in other potentials for biomedical applications. Furthermore, the adsorption of a single protein from mixtures based on size- and shape-selective separation can open up new ways to produce micro-objects that suit a given protein encapsulation design.

    Original languageEnglish
    Pages (from-to)288-297
    Number of pages10
    JournalColloids and Surfaces B: Biointerfaces
    Volume103
    DOIs
    Publication statusPublished - 2013 Mar 1

    Fingerprint

    Aluminum Oxide
    Alumina
    aluminum oxides
    proteins
    Proteins
    Adsorption
    adsorption
    Encapsulation
    genes
    Genes
    Technology
    Galectin 3
    Lactoglobulins
    Porins
    porosity
    myosins
    insulin
    Amylases
    Myosins
    Muramidase

    Keywords

    • Bioadsorbents
    • Langmuir adsorption isotherms
    • Mesocage alumina
    • Protein
    • Theoretical models

    ASJC Scopus subject areas

    • Biotechnology
    • Colloid and Surface Chemistry
    • Physical and Theoretical Chemistry
    • Surfaces and Interfaces

    Cite this

    Bioadsorption of proteins on large mesocage-shaped mesoporous alumina monoliths. / El-Safty, Sherif A.; Shenashen, M. A.; Khairy, M.

    In: Colloids and Surfaces B: Biointerfaces, Vol. 103, 01.03.2013, p. 288-297.

    Research output: Contribution to journalArticle

    El-Safty, Sherif A. ; Shenashen, M. A. ; Khairy, M. / Bioadsorption of proteins on large mesocage-shaped mesoporous alumina monoliths. In: Colloids and Surfaces B: Biointerfaces. 2013 ; Vol. 103. pp. 288-297.
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