Document Type : Research Paper

Authors

• Sama J. Al-zuwaini ¹
• Faramarz Mehrnejad ²
• Yasaman Mahmoodi ³
• Ali Hossein Rezayan ⁴
• Mohammad Barshan-tashnizi ⁴

¹ Department of Life Science Engineering, Faculty of New Sciences and Technology, University of Tehran, Tehran, Iran.

² Department of Life Science Engineering, Faculty of New Sciences and Technologies, University of Tehran, Tehran, Iran.

³ Life Science Engineering, Faculty of New Sciences and Technologies, University Of Tehran, Tehran, Iran

⁴ Department of Life Science Engineering, Faculty of New Sciences and Technology, University of Tehran, Tehran, Iran

Abstract

The enzyme L-asparaginase is widely used as complementary chemotherapy and an enzymatic drug to treat many diseases. However, as a medication, L-asparaginase also faces difficulties because of the inherent nature of proteins. As a result, various natural and synthetic polymers are used to create biodegradable nanospheres and microspheres for drug delivery and release. In this study, the effect of poly (lactic acid) (PLA) on the structure and dynamics of L-asparaginase was studied using molecular dynamics (MD) simulations. The results showed that the secondary and tertiary structures of the protein in the presence of the polymer did not change during the simulation time and even increased the stability of the structure and decreased the protein dynamics. This study showed that lysine and arginine actively interact with the PLA polymers. Several hydrophobic and polar amino acids interact with the polymer and the enzyme. The results showed that the main binding forces of PLA polymer to L-asparaginase are electrostatic and van der Waals interactions. The findings of this study can provide useful information to clarify some of the ambiguities in the experimental results for the encapsulation of the enzyme L-asparaginase and its use in the pharmaceutical industry.

Keywords

• L-asparaginase
• Encapsulation
• PLA
• Molecular dynamics simulation
• Self-assembly

Main Subjects

• Biophysics