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A study of the binding between polymers and peptides, using affinity capillary electrophoresis, applied to polymeric drug delivery systems
Author(s) -
Progent Frédéric,
Taverna Myriam,
Le Potier Isabelle,
Gopée Frédéric,
Ferrier Danielle
Publication year - 2002
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/1522-2683(200203)23:6<938::aid-elps938>3.0.co;2-7
Subject(s) - capillary electrophoresis , chemistry , chromatography , peptide , polymer , capillary action , binding constant , adsorption , linearization , analytical chemistry (journal) , binding site , nonlinear system , thermodynamics , biochemistry , organic chemistry , physics , quantum mechanics
We have investigated the potential of affinity capillary electrophoresis (ACE) to evaluate binding constants between an anionic polydispersed polymer and four peptides. Nonlinear regression and three current linearization methods, the y ‐reciprocal, the x ‐reciprocal and the double‐reciprocal, were employed for the estimation of the binding constants. The x ‐reciprocal and the double‐reciprocal plots indicated the presence of two portions of straight lines for angiopeptin, triptorelin and the thyrotropin releasing hormone (TRH), and therefore the probable existence of a second‐order interaction which causes the deviation from the 1:1 model. Peptide 1 exhibited a unique binding constant of 2.4×10 6 M –1 . In contrast, angiopeptin, triptorelin and TRH exhibited a K 1 of 4.0×10 6 , 5.3×10 6 and 20.2×10 6 M –1 , respectively, and a K 2 of 0.4×10 6 , 0.5×10 6 and 1.4×10 6 M –1 , respectively. The origin of the high scattering of the data points was further investigated. Neither the viscosity, nor the adsorption of the peptides to the capillary wall appeared to be the determining factor of data scattering. Finally, a possible adsorption of the polymer leading to the electroosmotic flow unstability was supposed.