Open AccessGeneral Method for Peptide Recognition in Water through Bioinspired Complementarity
Author(s) -
Shixin Fa,
Yan Zhao
Publication year - 2019
Publication title -
chemistry of materials
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.741
H-Index - 375
eISSN - 1520-5002
pISSN - 0897-4756
DOI - 10.1021/acs.chemmater.9b01613
Subject(s) - peptide , chemistry , tripeptide , molecular recognition , combinatorial chemistry , affinities , binding selectivity , monomer , selectivity , biomolecule , structural motif , plasma protein binding , biophysics , stereochemistry , biochemistry , polymer , molecule , organic chemistry , biology , catalysis
A general method for peptide recognition has been elusive despite decades of research. Strong binding and selectivity among closely related peptides are necessary for biological applications but have been difficult to achieve with synthetic receptors. With inspiration from highly specific protein-protein and protein-ligand interactions, protein-sized, water-soluble imprinted nanoparticles were prepared via templated polymerization of peptides within cross-linked micelles. Combination of hydrophobic and polar interactions afforded micromolar to submicromolar binding affinities for selected tripeptides. A "golden pair" of functional monomers was identified to enhance both the affinity and selectivity of binding, and enabled differentiation of subtly different sequences including single-point variation of lysine by arginine and insertion of a single glycine at the N- or C-terminus. Biological peptides (β-amyloid peptides) afforded even stronger binding (tens of nanomolar) due to a larger number of complementary interactions between the host and the guest, opening doors to a wide range of biological applications.