Abstract
The objective of the present study is to formulate and characterize a nanoparticulate-based formulation of a macromolecule in a hydrophobic ion pairing (HIP) complex form. So far, HIP complexation approach has been studied only for proteins with molecular weight of 10–20 kDa. Hence, we have selected bovine serum albumin (BSA) having higher molecular weight (66.3 kDa) as a model protein and dextran sulphate (DS) as a complexing polymer to generate HIP complex. We have prepared and optimized the HIP complex formation process of BSA with DS. Ionic interactions between basic amino acids of BSA with sulphate groups of DS were confirmed by FTIR analysis. Further, nanoparticles were prepared and characterized with respect to size and surface morphology. We observed significant entrapment of BSA in nanoparticles prepared with minimal amounts of PLGA polymer. Finally, results of circular dichroism and intrinsic fluorescence assay have clearly indicated that HIP complexation and method of nanoparticle preparation did not alter the secondary and tertiary structures of BSA.
Highlights
Protein-based therapeutics such as antibodies, blood derived products, and vaccines have been widely investigated in the past decade to treat a variety of disorders [1]
We have investigated hydrophobic ion pairing (HIP) complex formation by employing dextran sulphate, a polysaccharide-based molecule
Standard and test samples were prepared in 10 mM Na2HPO4 solution
Summary
Protein-based therapeutics such as antibodies, blood derived products, and vaccines have been widely investigated in the past decade to treat a variety of disorders [1]. Protein-based therapeutics tend to exhibit rapid denaturation and conformational change due to sonication and exposure to organic solvents [2, 3]. These molecules may aggregate and eventually lose their biological activity due to physical and chemical stress observed during formulation development, for example, exposure to organic solvents and sonication. In presence of organic solvents, the native structure and conformation of the protein can be altered This process may result in loss of biological activity of a protein molecule. Higher amounts of PLGA can lower the stability of protein molecules as protein molecules were found to be unstable in presence of lactic acid
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