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Affinity sorbents containing benzamidine derivatives for biomedical application.

N I Lasionova, G V Mityushina, I V Beresin

    Die Pharmazie
    |November 1, 1984
    PubMed
    Summary

    New affinity sorbents effectively purify trypsin and show potential for treating acute pancreatitis by reducing blood proteases. Immobilized inhibitors demonstrate significant therapeutic promise.

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    Area of Science:

    • Biochemistry
    • Biomaterials Science
    • Medical Chemistry

    Background:

    • Trypsin plays a crucial role in various physiological processes.
    • Elevated trypsin levels are implicated in diseases like acute pancreatitis.
    • Developing efficient methods for trypsin purification and removal is clinically significant.

    Purpose of the Study:

    • To develop and characterize novel affinity sorbents for trypsin immobilization.
    • To evaluate the efficacy of these sorbents in purifying trypsin and in a preclinical model of acute pancreatitis.

    Main Methods:

    • Immobilization of 4-amidinophenylalkylcarboxylic acids onto macroporous silica gel.
    • Frontal chromatography to determine dissociation constants (Kd) of trypsin-inhibitor complexes.
    • Purification of commercial trypsin and hemoperfusion studies in dogs.

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    Main Results:

    • Immobilization increased the dissociation constant (Kd) of trypsin-inhibitor complexes by 50-100 fold.
    • The affinity sorbent successfully purified a commercial trypsin preparation.
    • Hemoperfusion in dogs with acute pancreatitis demonstrated the sorbent's ability to reduce blood proteases without affecting protease inhibitors.

    Conclusions:

    • Immobilized 4-amidinophenylalkylcarboxylic acids serve as effective affinity sorbents for trypsin.
    • The developed biospecific sorbent shows promise for therapeutic applications, such as treating acute pancreatitis by selectively removing excess proteases from blood.