Abstract
To increase the in vivo stability of bioactive proteins via optimized loading methods. β-Glucosidase (β-Glu), as a model protein, was immobilized on magnetic nanoparticles(denoted as MNP-β-Glu) by chemical coupling methods and was further modified by poly(ethylene glycol) (PEG) molecules (denoted as MNP-β-Glu-PEG) to increase its stability. The physicochemical properties of the as-prepared nanohybrids, including the particle size, zeta potential, and enzyme activity, were well characterized. The proper MNP/β-Glu feed ratio was important for optimizing the particle size. Analysis of enzyme activity showed that the stability of immobilized β-Glu compared with free β-Glu was lower in deionized water and higher in blood serum at 37°C. MNP-β-Glu-PEG retained 77.9% of the initial activity within 30days at 4°C, whereas the free enzyme retained only 58.2%. Pharmacokinetic studies of Sprague-Dawley (SD) rats showed that the MNP-β-Glu-PEG group retained a higher enzyme activity in vivo (41.46% after 50min) than the MNP-β-Glu group (0.03% after 50min) and the β-Glu group (0.37% after 50min). Moreover, in contrast to the MNP-β-Glu group, the enzyme activity was not fully synchronous with the decrease in the Fe concentration in the MNP-β-Glu-PEG group. All findings indicated that the method of immobilization on magnetic nanoparticles and PEG modification is promising for the application of bioactive proteins in vivo.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
