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Glyco-Ligated Binders to Lectins: Multivalency vs Specificity.

Roya Jafari¹, Petr Král^1,2

¹Department of Chemistry, University of Illinois Chicago, Chicago, Illinois 60607, United States.

The Journal of Physical Chemistry. B

|July 10, 2026

Summary

This summary is machine-generated.

Simple peptidoglycans show strong lectin-binding affinities, rivaling complex supramolecular structures. This study compares glycan binders, including metallosupramolecular glycoassemblies and peptidoglycans, to Concanavalin A (ConA).

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Area of Science:

Biochemistry
Molecular Biology
Biophysics

Background:

Lectins are carbohydrate-binding proteins crucial for biological recognition.
Concanavalin A (ConA) is a well-characterized plant lectin with affinity for mannose and glucose.
Understanding glycan-lectin interactions is vital for various biological processes.

Purpose of the Study:

To compare the binding affinities of different glycan-based binders to lectins.
To model and analyze metallosupramolecular glycoassemblies and peptidoglycans binding to ConA.
To investigate the influence of binder topology, charge, and linker length on binding.

Main Methods:

Atomistic molecular dynamics simulations were employed.
Metallosupramolecular glycoassemblies with varying properties were modeled.
A small peptidoglycan binder was designed and modeled.
Binding affinities to Concanavalin A (ConA) were analyzed.

Main Results:

Both metallosupramolecular glycoassemblies and peptidoglycans were modeled binding to ConA.
Simple peptidoglycans demonstrated strong binding affinities to ConA.
The binding strength of peptidoglycans was comparable to larger, multivalent supramolecular binders.
Binder characteristics like topology, core charge, and linker length influenced binding.

Conclusions:

Small peptidoglycans can exhibit potent lectin-binding capabilities.
The affinity of simple peptidoglycans rivals that of complex supramolecular structures.
This finding has implications for designing novel glycan-based recognition agents.