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RESEARCH FRONT
Contents Vol 67(12)

Inhibitors of Galectins and Implications for Structure-Based Design of Galectin-Specific Therapeutics

Helen Blanchard A B , Khuchtumur Bum-Erdene A and Matthew W. Hugo A
+ Author Affiliations
- Author Affiliations

A Institute for Glycomics, Griffith University, Gold Coast Campus, Queensland 4222, Australia.

B Corresponding author. Email: h.blanchard@griffith.edu.au




Associate Professor Helen Blanchard (Ph.D. (1990), Chemistry and small-molecule crystallography, University of London, UK) undertook post-doctoral research in protein X-ray crystallography and drug-design in academia and industry within Canada, USA, Switzerland and Australia. In 2002 Helen established a protein X-ray crystallography structural biology group at the Institute for Glycomics, Griffith University. As recognition of her international contribution to structural biology and chemistry she was admitted as fellow of the Royal Society of Chemistry (FRSC) in 2006. Her research involves determination of atomic protein structure, analysis of protein-ligand interactions and application of this information in understanding protein function and for structure based drug-design. Her research group has a major focus on lectins critical to disease progression including her research program on galectins that have importance in serious conditions including cancer.


Khuchtumur Bum-Erdene completed his Bachelors degree in Chemistry (2010) at Indiana University-Purdue University Indianapolis in USA and is a Ph.D. student at the Institute for Glycomics, Griffith University under the supervision of Associate Professor Helen Blanchard. His research focuses on the structure-function of the galectin family of proteins and structure-based drug design.


Matt Hugo completed his Bachelor of Biomolecular Science (Advanced) with Honours (2013) at Griffith University and is a Ph.D. student under the supervision of Associate Professor Helen Blanchard at the Institute for Glycomics, Griffith University. His research encompasses structure-based drug design and synthesis of inhibitors targeting galectins.

Australian Journal of Chemistry 67(12) 1763-1779 https://doi.org/10.1071/CH14362
Submitted: 6 June 2014  Accepted: 10 July 2014   Published: 29 September 2014

Abstract

Galectins are a family of galactoside-specific lectins that are involved in a myriad of metabolic and disease processes. Due to roles in cancer and inflammatory and heart diseases, galectins are attractive targets for drug development. Over the last two decades, various strategies have been used to inhibit galectins, including polysaccharide-based therapeutics, multivalent display of saccharides, peptides, peptidomimetics, and saccharide-modifications. Primarily due to galectin carbohydrate binding sites having high sequence identities, the design and development of selective inhibitors targeting particular galectins, thereby addressing specific disease states, is challenging. Furthermore, the use of different inhibition assays by research groups has hindered systematic assessment of the relative selectivity and affinity of inhibitors. This review summarises the status of current inhibitors, strategies, and novel scaffolds that exploit subtle differences in galectin structures that, in conjunction with increasing available data on multiple galectins, is enabling the feasible design of effective and specific inhibitors of galectins.


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