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A Supramolecular Vesicle Based on the Complexation of p ‐Sulfonatocalixarene with Protamine and its Trypsin‐Triggered Controllable‐Release Properties
Author(s) -
Wang Kui,
Guo DongSheng,
Zhao MengYao,
Liu Yu
Publication year - 2016
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201303963
Subject(s) - trypsin , supramolecular chemistry , protamine , chemistry , vesicle , cationic polymerization , serine protease , enzyme , protease , combinatorial chemistry , biochemistry , molecule , organic chemistry , membrane , heparin
Enzyme‐responsive assembly represents one of the increasingly significant topics in biomaterials research and finds feasible applications to the controlled release of therapeutic agents at specific sites at which the target enzymes are located. In this work, based on the concept of host–guest chemistry, a trypsin‐responsive supramolecular vesicle using p ‐sulfonatocalix[4]arene as the macrocyclic host and natural serine protease trypsin‐cleavable cationic protein protamine as the guest molecule, is reported. The complexation of p ‐sulfonatocalix[4]arene with protamine directs the formation of a supramolecular binary vesicle, which is dissipated by trypsin with high selectivity. Therefore, the present system represents a principle‐of‐concept to build a controlled‐release carrier at trypsin‐overexpressed sites.