All Publications


  • Selective Array-Based Sensing of Anabolic Steroids in Aqueous Solution by Host-Guest Reporter Complexes CHEMISTRY-A EUROPEAN JOURNAL Gill, A. D., Perez, L., Salinas, I. N. Q., Byers, S. R., Liu, Y., Hickey, B. L., Zhong, W., Hooley, R. J. 2019; 25 (7): 1740-1745

    Abstract

    Arrayed complexes of a water-soluble deep cavitand and two fluorescent indicators show selective sensing of anabolic-androgenic steroids in aqueous environments. By combining the host-guest complexes with small amounts of heavy metal ions, discrimination between steroids that vary in structure by only a single π bond is possible. The sensing occurs through a triggered aggregation mechanism, which can be mediated by both the presence of metal ions and the steroids. The use of both "turn-on" and "turn-off" fluorophores is essential for good discrimination. As low as 10 μm steroid can be detected, and the discrimination is selective in steroid samples spiked into human urine.

    View details for DOI 10.1002/chem.201804854

    View details for Web of Science ID 000459811300019

    View details for PubMedID 30427566

  • Selective protein recognition in supported lipid bilayer arrays by tailored, dual-mode deep cavitand hosts SOFT MATTER Perez, L., Mettry, M., Hinman, S. S., Byers, S. R., McKeating, K. S., Caulkins, B. G., Cheng, Q., Hooley, R. J. 2017; 13 (21): 3966-3974

    Abstract

    Self-folding deep cavitands with variably functionalized upper rims are able to selectively immobilize proteins at a biomimetic supported lipid bilayer surface. The immobilization process takes advantage of the dual-mode binding capabilities of the hosts, combining a defined binding pocket with upper rim charged/H-bonding groups. A variety of proteins can be selectively immobilized at the bilayer interface, either via complementary charge/H-bonding interactions, cavity-based molecular recognition, or a combination of both. The immobilization process can be used to bind unmodified native proteins, epitopes for bioadhesion, or proteins covalently modified with suitable RNMe3+ binding "handles" and charged groups that can either match or mismatch with the cavitand rim. The immobilization process can be monitored in real time using surface plasmon resonance (SPR) spectroscopy, and applied to the construction of cavitand:lipid arrays using the hosts and trehalose vitrified phospholipid vesicles. The selective, dual-mode protein recognition is maintained in the arrays, and can be visualized using SPR imaging.

    View details for DOI 10.1039/c7sm00192d

    View details for Web of Science ID 000402744100015

    View details for PubMedID 28512660

    View details for PubMedCentralID PMC6041475

  • Site selective reading of epigenetic markers by a dual-mode synthetic receptor array CHEMICAL SCIENCE Liu, Y., Perez, L., Mettry, M., Gill, A. D., Byers, S. R., Easley, C. J., Bardeen, C. J., Zhong, W., Hooley, R. J. 2017; 8 (5): 3960-3970

    Abstract

    Variably functionalized self-folding deep cavitands form an arrayed, fluorescent indicator displacement assay system for the detection of post-translationally modified (PTM) histone peptides. The hosts bind trimethyllysine (KMe3) groups, and use secondary upper rim interactions to provide more sensitive discrimination between targets with identical KMe3 binding handles. The sensor array uses multiple different recognition modes to distinguish between miniscule differences in target, such as identical lysine modifications at different sites of histone peptides. In addition, the sensor is affected by global changes in structure, so it is capable of discriminating between identical PTMs, at identical positions on amino acid fragments that vary only in peptide backbone length, and can be applied to detect non-methylation modifications such as acetylation and phosphorylations located multiple residues away from the targeted binding site. The synergistic application of multiple variables allows dual-mode deep cavitands to approach levels of recognition selectivity usually only seen with antibodies.

    View details for DOI 10.1039/c7sc00865a

    View details for Web of Science ID 000400553000079

    View details for PubMedID 28553538

    View details for PubMedCentralID PMC5433514