Matching pH values for antibody stabilization and crystallization suggest rationale for accelerated development of biotherapeutic drugs.

Monoclonal antibodies (mAbs) are currently leading products in the global biopharmaceutical market. Multiple mAbs are in clinical development and novel biotherapeutic protein scaffolds, based on the canonical immunoglobulin G (IgG) fold, are emerging as treatment options for various medical conditions. However, fast approvals for biotherapeutics are challenging to achieve, because of difficult scientific development procedures and complex regulatory processes.

Standardization of the Reconstitution Procedure of Protein Lyophilizates as a Key Parameter to Control Product Stability.

Lyophilization of protein formulations is an essential tool for stabilization and is becoming increasingly important for pharmaceutical development. Reconstitution of the lyophilized cakes is crucial to obtain an applicable product. Nowadays, manual reconstitution by patients or medical staff is the common method defined in instructions for marketed lyophilized drug products.

Protein-Excipient Interactions Evaluated via Nuclear Magnetic Resonance Studies in Polysorbate-Based Multidose Protein Formulations: Influence on Antimicrobial Efficacy and Potential Study Approach.

Preservatives are excipients essentially needed in pharmaceutical multidose formulations to prevent microbial growth. Among available substances, phenol is widely used for parenterals; however, it is known to interact with nonionic surfactants like polysorbate and potentially with the active pharmaceutical ingredient. Although the need for combinations of surfactants and preservatives is growing, to date possible molecular interactions which can eventually weaken the stability and antimicrobial activity of the formulation are not yet well understood and properly investigated.

Non-aqueous suspensions of antibodies are much less viscous than equally concentrated aqueous solutions.

Purpose: The aim of this study was to markedly lower the viscosities of highly concentrated protein, in particular antibody, formulations. An effective approach elaborated herein for γ-globulin and a monoclonal antibody is to replace aqueous solutions with equimolar suspensions in neat organic solvents.

Methods: Viscosities of aqueous solutions and non-aqueous suspensions of the model protein bovine γ-globulin and a murine monoclonal antibody were examined under a variety of experimental conditions.