TY - JOUR
T1 - Effect of encapsulating arginine containing molecules on PLGA: A solid-state NMR study
AU - Guilbaud, Jean-Baptiste
AU - Baker, Helen
AU - Clark, Brian C.
AU - Meehan, Elisabeth
AU - Khimyak, Yaroslav Z.
PY - 2010/6
Y1 - 2010/6
N2 - Design of polymer–drug composites based on the lactide/glycolic acid often rely on the chemical complementarity between the polymer and functional groups in a pharmaceutical guest. We previously characterised decapeptide (AZD)/poly(D,L-lactide-co-glycolide) (PLGA) film formulations aiming at localising the interacting groups responsible for the changes in the bulk properties of the polymer matrix and understanding the mechanism of stabilisation of the drug into the polymer matrix. The results suggested interactions to occur between the arginine residue in the peptide and the carbonyl end group of the polymer chains. In order to clarify the role of arginine in directing the drug–polymer interactions, arginine and hexapeptide containing arginine were encapsulated in a PLGA 50/50 polymer. Variable temperature measurements and WISE experiments indicated significant changes in the local dynamics of the polymer chains. These effects were enhanced near and above Tg suggesting the presence of guests promote the appearance of backbone motion of the polymer chains. The localisation of the interactions on the carbonyl groups of the polymer was further confirmed by the WISE experiments. © 2009 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 99: 2697–2710, 2010
AB - Design of polymer–drug composites based on the lactide/glycolic acid often rely on the chemical complementarity between the polymer and functional groups in a pharmaceutical guest. We previously characterised decapeptide (AZD)/poly(D,L-lactide-co-glycolide) (PLGA) film formulations aiming at localising the interacting groups responsible for the changes in the bulk properties of the polymer matrix and understanding the mechanism of stabilisation of the drug into the polymer matrix. The results suggested interactions to occur between the arginine residue in the peptide and the carbonyl end group of the polymer chains. In order to clarify the role of arginine in directing the drug–polymer interactions, arginine and hexapeptide containing arginine were encapsulated in a PLGA 50/50 polymer. Variable temperature measurements and WISE experiments indicated significant changes in the local dynamics of the polymer chains. These effects were enhanced near and above Tg suggesting the presence of guests promote the appearance of backbone motion of the polymer chains. The localisation of the interactions on the carbonyl groups of the polymer was further confirmed by the WISE experiments. © 2009 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 99: 2697–2710, 2010
U2 - 10.1002/jps.22019
DO - 10.1002/jps.22019
M3 - Article
VL - 99
SP - 2697
EP - 2710
JO - Journal of Pharmaceutical Sciences
JF - Journal of Pharmaceutical Sciences
SN - 0022-3549
IS - 6
ER -