Heparin-binding of the human chitinase-like protein YKL-40 is allosterically modified by chitin oligosaccharides

Unnur Magnusdottir*, Finnbogi R. Thormodsson, Lilja Kjalarsdottir, Hordur Filippusson, Johannes Gislason, Kristinn Ragnar Oskarsson, Jens G. Hjorleifsson, Jon M. Einarsson

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

The chitinase-like protein YKL-40 (CHI3L1) has been implicated in the pathophysiology of inflammation and cancer. Recent studies highlight the growing interest in targeting and blocking the activity of YKL-40 to treat cancer. Some of those targeting-strategies have been developed to directly block the heparin-affinity of YKL-40 with promising results. This study explores how short chain chitooligosaccharides (ChOS) affect the heparin-binding affinity of YKL-40. Our findings reveal that ChOS act as allosteric effectors, decreasing the heparin-binding affinity of YKL-40 in a size- and dose-dependent manner. Our results provide insights into the heparin affinity of YKL-40 and how ChOS can be used to target the heparin activity of YKL-40 in diseases. Since ChOS has many beneficial properties, such as being non-toxic and biodegradable, these results provide intriguing opportunities for applying them as allosteric effectors of the heparin-binding affinity of YKL-40.

Original languageEnglish
Article number101908
JournalBiochemistry and Biophysics Reports
Volume41
DOIs
Publication statusPublished - Mar 2025

Bibliographical note

Publisher Copyright:
© 2024 The Authors

Other keywords

  • Allostery
  • Binding affinity
  • Chitin oligosaccharides
  • Conformational change
  • Heparin
  • YKL-40

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