Hong, J.I., Namgoong, S.K., Bernardi, A. and Still, W.C. (1991) Highly Selective Binding of Simple Peptides by a C3 Macrotricyclic Receptor. Journal of the American Chemical Society, 113, 5111-5112.
http://dx.doi.org/10.1021/ja00013a084

has been cited by the following article:

• TITLE: An Assay Study of Molecular Recognition of Amino Acids in Water: Covalent Imprinting of Cysteine

  AUTHORS: Harsha Vardhan Reddy Burri, Donghong Yu

  KEYWORDS: Synthetic Receptor-Like Structure, Molecularly Imprinted Polymers, Thiol-Disulfide Exchange Based Recognition, Covalent Recognition

  JOURNAL NAME: Journal of Biomedical Science and Engineering, Vol.8 No.12, December 17, 2015

  ABSTRACT: A novel synthetic N-(9-fluorenyl methoxy carbonyl)-L-Cysteine (Fmoc-Cys(SH)-OH) receptor was pre- pared by co-polymerizing (9-fluorenyl methoxy carbonyl)-S-(1-propene-2-thiol)-L-Cysteine (Fmoc-Cys(SCH2CHCH2)-OH) and a non-imprinted polymer prepared from 1-propene-1-thiol photo-chemically 15 h at room temperature and additional 3 h thermally at 80℃. Subsequently, disulfides were reduced with lithium aluminum hydride (LiAlH4) from imprinted polymers. The imprinted polymers selectively recognized Fmoc-Cys(SH)-OH with high binding constants in aqueous and protic solvents by thiol-disulfide exchange reactions. In order to estimate the covalent rebinding, particles were further extracted and disulfides reduced were estimated with the non-covalent recognized and covalently bounded analytes. From rebinding studies that were conducted, we observed that proved polymer particles could be reproducible and contain constant binding strengths and recognition properties. Furthermore, we proved that short incubation periods resulted in fast and efficient thiol-disulfide interchange reactions.