Design and Development of Divalent Lectin Ligands

Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

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 languageEnglish
Title of host publicationComprehensive Glycoscience
EditorsJoseph J. Barchi, Jr.
PublisherElsevier
Chapter3.17
Pages405-413
Number of pages9
Volume3
Edition2
ISBN (Print)978-0-12-822244-7
DOIs
Publication statusPublished - 24 Jun 2021

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