AL-zuwaini, Sama J.
[Verfasser:in];
Mehrnejad, Faramarz
[Verfasser:in];
Lotfi-Sousefi, Zahra
[Verfasser:in];
Rezayan, Ali Hossein
[Verfasser:in];
Barshan‐Tashnizi, Mohammad
[Verfasser:in]
The Process of L-Asparaginase Encapsulation by Poly (Lactic-Co-Glycolic Acid) and Methoxy Poly (Ethylene Glycol)
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Medientyp:
E-Book
Titel:
The Process of L-Asparaginase Encapsulation by Poly (Lactic-Co-Glycolic Acid) and Methoxy Poly (Ethylene Glycol)
:
A Molecular Dynamics Simulation Study
Beschreibung:
L-asparaginase (ASNase) is an enzyme that catalyzes the hydrolysis of L-asparagine to L-aspartic acid and ammonia. Because L-asparaginase suppresses protein synthesis in tumor cells, it is widely used in pediatric chemotherapy to treat children with acute lymphocytic leukemia (ALL). However, L-asparaginase, currently licensed by US Food and Drug Administration (FDA), is highly immunogenic, generating toxicities in more than half of cancer cases. L-asparaginase, as a medication, also faces difficulties because of the inherent nature of proteins. As a result, various natural and synthetic polymers are employed to create protein-loaded biodegradable nano and microspheres. The impact of biocompatible synthetic polymers such as methoxy poly (ethylene glycol) (MPEG) and poly (lactic-co-glycolic acid) (PLGA) copolymers on the structure and dynamics of L-asparaginase (EcAII) were studied using molecular dynamics (MD) simulations in this study. The results showed that the protein was more stable in PLGA than in MPEG, where electrostatic interactions were the major driving mechanism for associating EcAII and PLGA. At the same time, the hydrophobic and vdW interactions provide the driving force for the protein-MPEG interaction. The MD results further demonstrate that the protein's basic residues actively interact with the PLGA polymer and play critical roles in the encapsulated mechanism, whereas MPEG only partially encapsulates the protein. The protein's structure, on the other hand, was preserved throughout encapsulation. We anticipate that the findings of this study will contribute to our understanding of how L-asparaginase interacts with various polymers and copolymers used in medication administration