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Protein Complexation and pH Dependent Release Using Boronic Acid Containing PEG‐Polypeptide Copolymers
Author(s) -
Negri Graciela E.,
Deming Timothy J.
Publication year - 2017
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.201600136
Subject(s) - phenylboronic acid , copolymer , chemistry , ethylene glycol , boronic acid , polymer chemistry , amine gas treating , peg ratio , lysine , side chain , amino acid , biochemistry , combinatorial chemistry , organic chemistry , polymer , finance , economics , catalysis
New poly(L‐lysine)‐ b ‐poly(ethylene glycol) copolypeptides have been prepared, where the side‐chain amine groups of lysine residues are modified to contain ortho‐amine substituted phenylboronic acid, i.e., Wulff‐type phenylboronic acid (WBA), groups to improve their pH responsive, carbohydrate binding properties. These block copolymers form nanoscale complexes with glycosylated proteins that are stable at physiological pH, yet dissociate and release the glycoproteins under acidic conditions, similar to those found in endosomal and lysosomal compartments within cells. These results suggest that WBA modified polypeptide copolymers are promising for further development as degradable carriers for intracellular protein delivery.