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1 H NMR Study of “Host–Guest” Interactions of Micellar Assemblies from Amphiphilic Invertible Polymers and Peptides
Author(s) -
Kohut Ananiy,
Zholobko Oksana,
Hevus Ivan,
Voronov Andriy
Publication year - 2017
Publication title -
macromolecular chemistry and physics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.57
H-Index - 112
eISSN - 1521-3935
pISSN - 1022-1352
DOI - 10.1002/macp.201700344
Subject(s) - amphiphile , peptide , chemistry , polymer , aqueous solution , polymer chemistry , self assembly , molecule , combinatorial chemistry , organic chemistry , copolymer , biochemistry
“Host–guest” interactions between self‐assembled micellar nanostructures from amphiphilic invertible polymers (AIPs) and two peptides, swine‐origin Influenza A surface protein Hemagglutinin and research antibody peptide V5, are investigated by changing the polymer concentration and polymer/peptide ratio in the aqueous solution. Formation of mixed micellar assemblies from AIP and each peptide is revealed using detailed 1 H NMR spectroscopic study. Peptide molecule localization in the micellar assemblies depends on the specific interactions between amino acid functional groups of the peptide and polymer fragments. The resulting mixed micellar structures can be considered as a promising material toward delivery and stimuli‐responsive sustained release of peptides.