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Updated: Jun 21, 2025

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
In silico approaches for better understanding cysteine cathepsin-glycosaminoglycan interactions
Krzysztof K Bojarski1, Alexis David2, Fabien Lecaille2
1Department of Physical Chemistry, Gdansk University of Technology, Narutowicza 11/12, Gdansk, 80-233, Poland.
Abstract:
Cysteine cathepsins constitute the largest cathepsin family, with 11 proteases in human that are present primarily within acidic endosomal and lysosomal compartments. They are involved in the turnover of intracellular and extracellular proteins. They are synthesized as inactive procathepsins that are converted to mature active forms. Cathepsins play important roles in physiological and pathological processes and, therefore, receive increasing attention as potential therapeutic targets. Their maturation and activity can be regulated by glycosaminoglycans (GAGs), long linear negatively charged polysaccharides composed of recurring dimeric units. In this review, we summarize recent computational progress in the field of (pro)cathepsin-GAG complexes analyses.
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