Nonionic surfactants like Polysorbate 20, Polysorbate 80, and Poloxamer 188 are essential in preventing antibody aggregation and adsorption in biopharmaceutical formulations. Our work compares the interfacial activity and biopharmaceutical stability of Kolliphor® HS 15, using techniques such as tensiometry, interfacial rheology, and QCM-D. Results reveal notable differences among surfactants and highlight the impact of interface type. Additional tests assessed protein aggregation, oil release from siliconized vials, and surfactant stability against enzymatic degradation. Kolliphor® HS 15 matches polysorbates in interfacial activity and stabilization and shows a comparable resistance to enzymatic degradation with advantages for certain model enzymes and maintains stability under oxidative stress. Kolliphor® P188, though less active at interfaces, prevents aggregation of some proteins, suggesting multiple stabilization mechanisms and is therefore a suitable alternative These findings enhance understanding of surfactant-driven protein stabilization in various packaging systems.

Glucagon-like peptide 1 (GLP 1) analogues enhance insulin secretion, delay gastric emptying, and promote satiety, making them effective therapeutics for type 2 diabetes and obesity [1],[2]. Structural modifications have enabled GLP 1 agonists with markedly prolonged half lives, including semaglutide (SMG), which reaches approximately 180 hours and is currently administered via subcutaneous injection or oral tablets.

Although clinically effective, these routes present challenges such as the need for cold-chain storage and limited oral bioavailability. Developing a dry powder inhalation (DPI) formulation could provide a more patient friendly delivery option by enabling non invasive, portable, and potentially room temperature stable administration. However, as a peptide therapeutic, SMG requires careful consideration of stability in solution, compatibility with excipients, and protection during spray drying.

This work aimed to develop a spray dried SMG powder for inhalation that maintains peptide integrity while achieving suitable aerodynamic performance for deep lung delivery. A pre formulation study was conducted to evaluate buffer type and concentration in the feed solution, as well as excipient systems capable of stabilizing SMG throughout processing. These investigations identified conditions that support both chemical stability and the generation of respirable spray dried particles. The resulting data establish a foundation for advancing SMG DPI formulations as a more convenient and patient centric alternative to current delivery modalities.

Learning Objectives: 

1. Inform potential customers about Inhalation as a drug delivery option for biologics and peptides.

2. Describe the role of buffer systems and excipients in maintaining peptide integrity during spray drying.

3. Evaluate the unmet patient needs that motivate alternative delivery approaches such as DPI.