Skip to main content
Article
Boronic Acid Functionalized Peptidyl Synthetic Lectins: Combinatorial Library Design, Peptide Sequencing, and Selective Glycoprotein Recognition
ACS Combinatorial Science (2011)
  • Kevin L. Bicker, University of South Carolina
  • Jing Sun, Georgia Southern University
  • John J. Lavigne, University of South Carolina
  • Paul R. Thompson, University of South Carolina
Abstract
Aberrant glycosylation of cell membrane and secreted glycoproteins is a hallmark of various disease states, including cancer. The natural lectins currently used in the recognition of these glycoproteins are costly, difficult to produce, and unstable toward rigorous use. Herein we describe the design and synthesis of several boronic acid functionalized peptide-based synthetic lectin (SL) libraries, as well as the optimized methodology for obtaining peptide sequences of these SLs. SL libraries were subsequently used to identify SLs with as high as 5-fold selectivity for various glycoproteins. SLs will inevitably find a role in cancer diagnostics, given that they do not suffer from the drawbacks of natural lectins and that the combinatorial nature of these libraries allows for the identification of an SL for nearly any glycosylated biomolecule.
Keywords
  • Boronic acids,
  • Aberrant glycosylation,
  • Synthetic lectins,
  • Cancer,
  • Sensors
Disciplines
Publication Date
2011
Publisher Statement
This is an Accepted Author Manuscript obtained from PMC. The publisher's final edited version of this article is available at ACS Combinatorial Science.
Citation Information
Kevin L. Bicker, Jing Sun, John J. Lavigne, and Paul R. Thompson. "Boronic Acid Functionalized Peptidyl Synthetic Lectins: Combinatorial Library Design, Peptide Sequencing, and Selective Glycoprotein Recognition" ACS Combinatorial Science 13.3 (2011): 232-243.
doi:10.1021/co100054e
source:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3090474/
Available at: http://works.bepress.com/jing_sun/4