American Chemical Society - Division of Carbohydrate Chemistry ...

CARB 93
Synthesis of tailored glycoconjugates for the precise detection of
pathogens
Ashish A. Kulkarni (1) , ashishkulkarni30@gmail.com, 506, Riddle Road,, Apt.
No. 41, Cincinnati Ohio 45220, United States ; Suri S. Iyer (1) . (1) Department of
Chemistry, University of Cincinnati, Cincinnati Ohio 45220, United States
Carbohydrate-protein interactions play a very important role in a variety of
essential biological processes such as adhesion, cell-cell communication and
organ differentiation. Several infectious agents use the cell surface
carbohydrates to gain entry and infect the cells. We are harnessing this
recognition capability and developing molecules that can be used as integral
components of biosensors. This work is highly significant because carbohydrates
are highly stable under a variety of conditions, do not suffer from lot-to-lot
variation, can be synthesized in large quantities and can be adapted to any
platform. Additionally, different strains, including newly emerging strains can be
identified rapidly. In this regard, we have developed chemically defined
glycoconjugates using a versatile modular approach for capturing toxins, viruses
and bacteria. Specifically, we have synthesized carbohydrate based recognition
elements and attached these molecules to a scaffold via flexible
oligoethylene glycol linkers. The multivalent unit has been covalently linked to a
fluorescent molecule or a biotin. The design and synthesis of these multivalent
ligands, covalent linkage of the scaffold to the ligands and the reporter to the
scaffold will be presented.
CARB 94
Structure-activity studies of synthetic glycophosphatidylinositol anchored
proteins
Carl V Christianson (1) , carl.christianson@mpikg.mpg.de, Free University Berlin,
Arnimallee 22, Berlin Berlin 12101, Germany ; Peter H Seeberger (1) . (1)
Department of Biomolecular Systems, Max Planck Institute of Colloids and
Interfaces, Berlin 12101, Germany
The structural complexity of glycophosphatidylinositol (GPI) anchors has
hindered studies relating structural elements to specific biological roles. Access
to defined GPI structures through total synthesis 1 facilitates the modification of
proteins via native chemical ligation (NCL) to probe the importance of
glycosylation and lipidation patterns of GPI anchors. 2 Here we present studies of
GFP modified with fully synthetic GPI anchors (Figure 1.) and other probes in
order to gain a better understanding of the role that this posttranslational
modification plays in
biological processes.