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Updated: Apr 18, 2026

Combinatorial Synthesis of and High-throughput Protein Release from Polymer Film and Nanoparticle Libraries

Combinatorial Synthesis of and High-throughput Protein Release from Polymer Film and Nanoparticle Libraries

Published on: September 6, 2012

Templating carbohydrate-functionalised polymer-scaffolded dynamic combinatorial libraries with lectins.

Clare S Mahon¹, Martin A Fascione, Chadamas Sakonsinsiri

¹Chemical Nanoscience Laboratory, School of Chemistry, Newcastle University, Newcastle-upon-Tyne, UK. david.fulton@ncl.ac.uk.

Organic & Biomolecular Chemistry

|January 20, 2015

Summary

This summary is machine-generated.

New polymer-scaffolded dynamic combinatorial libraries (PS-DCLs) adapt their composition to bind specific lectins. This molecular recognition enhances binding affinity through preferential carbohydrate incorporation and strategic residue reorganization.

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High-throughput Synthesis of Carbohydrates and Functionalization of Polyanhydride Nanoparticles

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Area of Science:

Biochemistry
Polymer Chemistry
Supramolecular Chemistry

Background:

Designing synthetic receptors for specific molecular recognition, particularly for carbohydrates, remains a significant challenge.
Dynamic combinatorial chemistry offers a powerful approach to generate molecular diversity and identify high-affinity binders.

Purpose of the Study:

To introduce a novel strategy for creating macromolecular receptors using polymer-scaffolded dynamic combinatorial libraries (PS-DCLs).
To demonstrate the ability of PS-DCLs to adapt their composition in response to lectin templates, leading to enhanced binding affinity.

Main Methods:

Preparation of PS-DCLs in aqueous solution via reversible conjugation of carbohydrate-acylhydrazides onto aldehyde-functionalised polymer scaffolds.
Exposure of PS-DCLs to specific lectin templates to induce compositional changes.
Affinity measurements to quantify the binding enhancements before and after templation.

Main Results:

PS-DCLs exhibited template-induced compositional changes, preferentially incorporating lectin-recognizing carbohydrate units.
Significant enhancements in binding affinity for the target lectins were observed, with free energy changes ranging from 5.2-8.8 kJ mol(-1).
Enhanced binding resulted from both increased display of preferred carbohydrates and strategic reorganization of polymer residues.

Conclusions:

PS-DCLs represent a conceptually new and effective approach for designing macromolecular receptors with tunable affinity for lectins.
The observed affinity enhancements highlight the synergistic effects of preferential binding unit display and structural reorganization induced by templation.