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Compatibility between Proteins and Polysaccharide Excipients in Oral Delivery Tablets.

Meng-Jia Jin1,2, Zhen-Yi Jing1,2, Li-Duo Liu1,3

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Sodium carboxymethyl starch (CMS) interacts electrostatically with proteins like trastuzumab (TRA), reducing soluble protein concentration. This interaction, dependent on pH, suggests CMS’s potential for sustained release of oral protein biopharmaceuticals.

Keywords:
biopharmaceutical tabletselectrostatic interactionmonoclonal antibody,polysaccharideproteinsodium carboxymethyl starch

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Area of Science:

  • Pharmaceutical Sciences
  • Biotechnology
  • Materials Science

Background:

  • Oral protein biopharmaceuticals are a growing research area.
  • Excipients used in small molecule drugs are often applied to protein formulations.
  • The interaction between proteins and excipients is often overlooked but critical for drug performance.

Purpose of the Study:

  • To investigate the interaction between proteins and sodium carboxymethyl starch (CMS), a common oral excipient.
  • To understand the impact of CMS on protein stability, solubility, and biological activity.
  • To explore the potential application of CMS in oral protein delivery systems.

Main Methods:

  • Size-exclusion high-performance liquid chromatography (SE-HPLC) to detect soluble protein concentration.
  • Enzyme-linked immunosorbent assay (ELISA) to assess biological activity.
  • Analysis of protein hydrophobicity and thermal stability.
  • Investigation of interactions with multiple proteins (trastuzumab, infliximab, etanercept) across various pH conditions.

Main Results:

  • Sodium carboxymethyl starch (CMS) caused a significant reduction in soluble trastuzumab (TRA) concentration, unlike other tested polysaccharides.
  • CMS exhibited an electrostatic interaction with TRA within a specific pH range, affecting protein monomer concentration, turbidity, hydrophobicity, and thermal stability.
  • This interaction was reversible, and protein solubility decreased significantly below the protein's isoelectric point due to electrostatic binding with negatively charged CMS.

Conclusions:

  • CMS strongly interacts electrostatically with proteins, particularly when the protein is positively charged (below its isoelectric point).
  • This reversible interaction suggests CMS could be utilized for sustained release formulations of oral protein biopharmaceuticals, including monoclonal antibodies.
  • Protein structural characteristics, such as surface charge and hydrophobicity, are crucial factors in selecting appropriate excipients for oral protein drug products.