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Peptide recognition by functional supramolecular nanopores with complementary size and binding sites 被引量:1
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作者 Yumin Chen Hui Nie +8 位作者 Ke Deng Shili Wu Jindong Xue Lijin Shu Yue Yu Yanfang Geng Ping Li Yanlian Yang Qingdao Zeng 《Nano Research》 SCIE EI CAS CSCD 2016年第5期1452-1459,共8页
The precise control of the conformations of biomolecules adsorbed on a surface at the single-molecule level is significant. However, it remains a huge challenge because of the complex structure and conformation divers... The precise control of the conformations of biomolecules adsorbed on a surface at the single-molecule level is significant. However, it remains a huge challenge because of the complex structure and conformation diversity of biomolecules. Herein, a "nanopore-confined recognition" strategy is proposed to manipulate the adsorption of individual valinomycin molecules at room temperature through precise design of functionalized conjugated macrocycle (CPN8) supramolecular nanopores with complementary architectures and binding sites. We revealed that CPN8 prefers to selectively recognizing valinomycin with complementary architecture because of the strong synergistic interactions between the isopropyl groups of valinomycin and the amino groups of CPN8, with valinomycin- highly oriented pyrolytic graphite (HOPG) interactions. Our perspectives at the single-molecule level will provide valuable insights to improve the design of supramolecular nanopores for conformation-selective recognition of non-conjugated molecules. 展开更多
关键词 host-vip recognition nanopore-confined scanning tunnelingmicroscopy shape-persistent macrocyde supramolecular assembly
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