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Effect of encapsulating arginine containing molecules on PLGA: a solid-state NMR study
Jean-Baptiste Guilbaud1, Helen Baker, Brian C Clark
1Department of Chemistry, The University of Liverpool, Crown St, Liverpool L69 7ZD, UK.
Journal of Pharmaceutical Sciences
|December 17, 2009
Summary
Arginine residues in peptides significantly alter polymer dynamics in poly(D,L-lactide-co-glycolide) composites. These interactions, localized at polymer carbonyl groups, enhance polymer backbone motion, crucial for drug stabilization.
Area of Science:
- Polymer science and drug delivery systems.
- Biomaterials and pharmaceutical formulation.
- Materials science and polymer dynamics.
Background:
- Polymer-drug composite design often depends on chemical complementarity.
- Previous studies suggested arginine in decapeptide (AZD) interacts with poly(D,L-lactide-co-glycolide) (PLGA) carbonyl end groups.
- Understanding these interactions is key to stabilizing drugs within polymer matrices.
Purpose of the Study:
- To elucidate the specific role of arginine in directing drug-polymer interactions.
- To investigate the impact of arginine-containing peptides on PLGA polymer dynamics.
- To confirm the localization of interactions between arginine and PLGA polymer chains.
Main Methods:
- Encapsulation of arginine and arginine-containing hexapeptide in PLGA 50/50 polymer.
- Variable temperature T1 rho H NMR measurements to assess molecular dynamics.
- Weakly Interacting Spin Echo (WISE) experiments to probe interaction localization.
Main Results:
- Significant changes in local polymer chain dynamics were observed with arginine-containing guests.
- These dynamic effects were amplified near and above the glass transition temperature (Tg).
- WISE experiments confirmed interactions are localized at the polymer's carbonyl groups.
Conclusions:
- Arginine plays a critical role in modulating polymer dynamics within PLGA composites.
- The presence of arginine-containing guests promotes polymer backbone motion, particularly above Tg.
- The findings confirm specific interactions between arginine residues and PLGA carbonyl groups, aiding drug stabilization mechanisms.

