2025/01/01 by Gillian Murphy, David L. Cheung, Michael Fitzgerald +1 · 1 voice
Biochemistry, Genetics and Molecular Biology · Medicine · Pharmacology, Toxicology and Pharmaceutics · #Advanced Drug Delivery Systems #Diabetes Treatment and Management #Protein Interaction Studies and Fluorescence Analysis
paper · pdf · doi:10.1016/j.csbj.2025.11.007
openalex publication_date 2025/01/01 · openalex created_date 2025/11/08 · openalex updated_date 2026/07/31
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. We quantified the binding energies, thermodynamics, conformational shifts and specific residue-interactions of the peptide-albumin complex. This study presents molecular-level findings on the relationship between these interactions and PEGylated hydrogel drug delivery systems, highlighting the potential translational applications of the in-silico model. Further research could lead to advancements in the design, development and characterization of such controlled release formulations and long-acting GLP-1 RA therapeutics. Moreover, this research suggests the possibility of harnessing MD simulations to design and develop biomaterial-based drug delivery devices for diabetes, among other disease indications.