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Glyco-Ligated Binders to Lectins: Multivalency vs Specificity
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DOI：10.1021/acs.jpcb.6c01091.png)
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Abstract
En 中文
Here, we examine and compare different types of glycan-based binders to lectins, a class of carbohydrate-binding proteins involved in many biological recognition processes. We use atomistic molecular dynamics simulations to model metallosupramolecular glycoassemblies of different topologies, core charges, and linker lengths binding in a multivalent manner to glyco-recognizing domains in Concanavalin A (ConA), a well-studied plant lectin with specific affinity for mannose and glucose. We also designed and modeled a small peptidoglycan specifically bound to ConA. The obtained results reveal that despite their small size, simple peptidoglycans can have strong affinities to lectins, comparable to large multivalent supramolecular binders.
Keywords:
Bioengineering and biotechnology
Carbohydrates
Ligands
Peptides and proteins
Receptors
Journal
T
IF:
2.9
Papers:
767
Citations:
2
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Cited Papers