In silico investigations of albumin-GLP-1 receptor agonist complexes for diabetes drug delivery applications

This paper describes the specific conformational folding patterns and residues involved in stabilizing the Glucagon-like Peptide-1 Receptor Agonist (GLP-1 RA) peptide-albumin protein complex using molecular dynamic (MD) simulations and surface plasmon resonance (SPR). We quantified the binding energies, thermodynamics, conformational shifts and specific residue-residue interactions of the peptide-albumin complex. The study presents molecular-level findings of the relationship between these interactions and the formation of amide bonds in a PEGylated hydrogel drug delivery system. This research outlines the potential of harnessing MD simulations as a biomaterial characterisation tool, giving deeper insights beyond the established <i>in vitro</i> methods. Further research in this field could lead to advancements in the rational design and development of next generation controlled release formulations and long-acting GLP-1 RA therapeutics.