GET THE APP

Model Protein-loaded PLGA Nanoparticles: A Scalable Production Process with Biocompatibility, Trafficking and Release Characteristics
..

Journal of Biomedical and Pharmaceutical Sciences

ISSN: 2952-8100

Open Access

Commentary - (2024) Volume 7, Issue 5

Model Protein-loaded PLGA Nanoparticles: A Scalable Production Process with Biocompatibility, Trafficking and Release Characteristics

Ribovski Ekhator*
*Correspondence: Ribovski Ekhator, Department of Pharmaceutics and Industrial Pharmacy, Ain Shams University, Cairo 11566, Egypt, Email:
Department of Pharmaceutics and Industrial Pharmacy, Ain Shams University, Cairo 11566, Egypt

Received: 02-Sep-2024, Manuscript No. jbps-25-159308; Editor assigned: 04-Sep-0204, Pre QC No. P-159308; Reviewed: 16-Sep-2024, QC No. Q-159308; Revised: 23-Sep-2024, Manuscript No. R-159308; Published: 30-Sep-2024 , DOI: 10.37421/2952-8100.2024.7.478
Citation: Ekhator, Ribovski. â??Model Protein-loaded PLGA Nanoparticles: A Scalable Production Process with Biocompatibility, Trafficking and Release Characteristics.â? J Biomed Pharm Sci 7 (2024): 478
Copyright: © 2024 Ekhator R. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Introduction

In recent years, protein therapeutics have emerged as a key player in the treatment of various diseases, ranging from cancer and autoimmune disorders to metabolic conditions and genetic diseases. However, despite their efficacy, the clinical application of proteins is hindered by several challenges, including poor bioavailability, instability and rapid clearance from the body. Nanotechnology has presented a promising solution to these challenges, particularly through the development of protein-loaded nanoparticles. Among the diverse range of nanoparticle systems, Poly(Lactic- Co-Glycolic Acid (PLGA) nanoparticles have gained significant attention due to their biocompatibility, biodegradability and ability to encapsulate a wide range of bioactive compounds, including proteins. This paper discusses the scalable production process of protein-loaded PLGA nanoparticles, focusing on their biocompatibility, trafficking and release characteristics.

Description

PLGA nanoparticles are one of the most widely studied nanocarriers for drug delivery due to their biocompatibility, ease of preparation and versatility. PLGA is a copolymer of lactic acid and glycolic acid, both of which are natural compounds metabolized by the body, making PLGA an ideal material for drug delivery applications. The primary advantage of PLGA nanoparticles lies in their ability to encapsulate and protect sensitive therapeutic agents, such as proteins, from enzymatic degradation and premature clearance. This allows for sustained and controlled release of the protein cargo over time, improving therapeutic efficacy and reducing the frequency of administration. Proteins, as therapeutic agents, offer significant advantages, such as high specificity and low toxicity, but their delivery faces numerous obstacles. The production process must meet several criteria, including reproducibility, scalability, costeffectiveness and the ability to maintain the structural integrity and bioactivity of the encapsulated protein. The scalability of the production process is particularly important for ensuring that protein-loaded nanoparticles can be manufactured in large quantities to meet the demands of clinical use or market commercialization [1,2]. Currently, various methods are used to prepare protein-loaded PLGA nanoparticles, such as solvent evaporation, coacervation and nanoprecipitation. Each method has its advantages and limitations and the choice of method depends on factors such as the type of protein, desired particle size and release characteristics. For large-scale production, the solvent evaporation method, in which PLGA is dissolved in an organic solvent and then emulsified in an aqueous phase, is often preferred due to its simplicity and ability to produce nanoparticles with good encapsulation efficiency. The biocompatibility of protein-loaded PLGA nanoparticles is a critical factor in determining their safety and effectiveness in vivo. PLGA is widely regarded as a biocompatible and biodegradable material due to its chemical structure and ability to be metabolized by the body. Once administered, PLGA nanoparticles are degraded by hydrolysis of the ester bonds in the polymer backbone, releasing lactic acid and glycolic acid, which are naturally occurring metabolites that are safely eliminated by the body.

Conclusion

Protein-loaded PLGA nanoparticles offer a promising solution for overcoming the challenges associated with protein therapeutics, including poor stability, rapid clearance and limited bioavailability. The therapeutic efficacy of proteins while minimizing side effects and improving patient compliance. The scalable production of protein-loaded PLGA nanoparticles is achievable using techniques such as solvent evaporation, nanoprecipitation and spray-drying, which can be adapted for large-scale manufacturing.The biocompatibility of PLGA nanoparticles, along with their efficient cellular uptake and controlled release characteristics, makes them a highly attractive platform for protein delivery. Further advancements in surface modification, targeting strategies and release profile control will enhance the clinical translation of protein-loaded PLGA nanoparticles, offering new possibilities for the treatment of a wide range of diseases.

References

  1. Hernando, Sara, Edorta Santos-Vizcaíno, Manoli Igartua and Rosa Maria Hernandez. "Targeting the central nervous system: From synthetic nanoparticles to extracellular vesicles-focus on Alzheimer's and Parkinson's disease." Wiley Interdiscip Rev Nanomed Nanobiotechnology 15 (2023): e1898.
  2. Google Scholar, Crossref, Indexed at

  3. Manders, E. M. M., J. Stap, G. J. Brakenhoff and R. van Driel, et al. "Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy." J Cell Sci 103 (1992): 857-862.
  4. Google Scholar, Crossref, Indexed at

arrow_upward arrow_upward