The selective removal of Zn from proteins by using a synthetic chelator is a promising therapeutic approach for the treatment of various diseases including cancer. Although the chelation of Zn is well known, its removal from a protein in the presence of potential competing biologically relevant ions such as Cu is hardly explored. Herein we present a peptoid - N-substituted glycine trimer - incorporating a picolyl group at the N-terminus, a non-coordinating but structurally directing benzyl group at the C-terminus and a 2,2':6',2''-terpyridine group in the second position, that selectively binds Zn ions in the presence of excess Cu ions in water. We further demonstrate that this chelator can selectively bind Zn from a pool of excess biologically relevant and competitive ions (Cu, Fe, Ca, Mg, Na, and K) in a simulated body fluid (SBF), and also its ability to remove Zn from a natural zinc protein domain (PYKPEGKSFSQKSDLVKQRTTG) in a SBF.
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| http://dx.doi.org/10.1039/d0sc03391j | DOI Listing |
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