Peptide recognition by functional supramolecular nanopores with complementary size and binding sites
host–guest recognition, nanopore-confined, scanning tunnelingmicroscopy, shape-persistent macrocycle, supramolecular assembly
The precise control of the conformations of biomolecules adsorbed on a surfaceat the single-molecule level is significant. However, it remains a huge challengebecause of the complex structure and conformation diversity of biomolecules.Herein, a “nanopore-confined recognition” strategy is proposed to manipulatethe adsorption of individual valinomycin molecules at room temperature throughprecise design of functionalized conjugated macrocycle (CPN8) supramolecularnanopores with complementary architectures and binding sites. We revealedthat CPN8 prefers to selectively recognizing valinomycin with complementaryarchitecture because of the strong synergistic interactions between the isopropylgroups of valinomycin and the amino groups of CPN8, with valinomycinhighlyoriented pyrolytic graphite (HOPG) interactions. Our perspectives at thesingle-molecule level will provide valuable insights to improve the design ofsupramolecular nanopores for conformation-selective recognition of non-conjugatedmolecules.
Tsinghua University Press
Yumin Chen,Hui Nie,Ke Deng,Shili Wu,Jindong Xue,Lijin Shu,Yue Yu,Yanfang Geng,Ping Li,Yanlian Yang,Qingdao Zeng, Peptide recognition by functional supramolecular nanopores with complementary size and binding sites. NanoRes.2016, 9(5): 1452–1459