IN SILICO ANALYSIS OF PROTEIN-EXCIPIENT INTERACTIONS: A MOLECULAR DOCKING STUDY ON THERAPEUTIC IL-11

Abstract

Interleukin-11 (IL-11) is a multifariously cytokine of great therapeutic interest, especially for hematopoiesis, inflammation, and management of fibrosis. Recombinant human IL-11 (rhIL 11) has been applied extensively in clinical use for the prevention of thrombocytopenia and other immune disorders. Nevertheless, the stability and bioactivity of IL-11 formulations are affected by their physical and chemical interaction with excipients during formulation. This study investigates the interactions of IL-11 with usual excipients, lactose, sucrose, trehalose, mannitol, and sorbitol using the molecular docking method. Binding affinities and interaction modes were thoroughly investigated to forecast the excipient function in stabilizing IL-11. Findings indicated that sugars such as lactose, trehalose, and sucrose exhibit higher binding interactions (-6.1, -5.8, and -6.0 kcal/mol) compared to sugar alcohols (mannitol and sorbitol), suggesting their viability as more efficient stabilizers for IL-11 in drug formulations. This computational strategy underpins the rational choice of excipients for cytokine stabilization and can inform future formulation design.