Abstract
Interference with protein carbohydrate interactions can potentially lead to many new therapeutics. However, challenges need to be overcome, one of which is weak affinity of glycoligands for their targets. Multivalent ligands can bind much more potent. Here we describe the road traveled toward potent divalent ligands for the Pseudomonas aeruginosa lectin LecA taking advantage of the most straightforward multivalency mechanism: chelation. Aspects of flexibility versus rigidity, thermodynamic parameters and molecular design are discussed.
Original language | English |
---|---|
Title of host publication | Comprehensive Glycoscience |
Editors | Joseph J. Barchi, Jr. |
Publisher | Elsevier |
Chapter | 3.17 |
Pages | 405-413 |
Number of pages | 9 |
Volume | 3 |
Edition | 2 |
ISBN (Print) | 978-0-12-822244-7 |
DOIs | |
Publication status | Published - 24 Jun 2021 |