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Related Experiment Video

Updated: Jun 21, 2026

Investigating Single Molecule Adhesion by Atomic Force Spectroscopy
09:48

Investigating Single Molecule Adhesion by Atomic Force Spectroscopy

Published on: February 27, 2015

Functionalized self-assembled monolayers for measuring single molecule lectin carbohydrate interactions.

Xiaojuan Zhang1, Vamsi K Yadavalli

  • 1Department of Chemical and Life Science Engineering, Virginia Commonwealth University, Richmond, VA, USA.

Analytica Chimica Acta
|August 12, 2009
PubMed
Summary

Researchers developed a new method to study single sugar-protein interactions using atomic force microscopy. This technique precisely measures the forces involved in lectin-carbohydrate binding, offering insights into biological functions.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Nanoscience

Background:

  • Specific interactions between lectins (sugar-binding proteins) and carbohydrates are crucial for many biological processes.
  • Understanding the molecular basis of these interactions is of significant scientific interest.

Purpose of the Study:

  • To develop an efficient method for fabricating carbohydrate arrays.
  • To investigate lectin-carbohydrate interactions at the single-molecule level using atomic force microscopy (AFM).
  • To determine the rupture force of single Concanavalin A (Con A)-mannose bonds.

Main Methods:

  • Fabrication of carbohydrate arrays using a one-step amination reaction and mixed self-assembled monolayers (SAMs).
  • Utilizing chemical force microscopy (CFM) to measure single-molecule bond rupture forces.

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A Technique to Functionalize and Self-assemble Macroscopic Nanoparticle-ligand Monolayer Films onto Template-free Substrates
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Last Updated: Jun 21, 2026

Investigating Single Molecule Adhesion by Atomic Force Spectroscopy
09:48

Investigating Single Molecule Adhesion by Atomic Force Spectroscopy

Published on: February 27, 2015

Antifouling Self-assembled Monolayers on Microelectrodes for Patterning Biomolecules
10:27

Antifouling Self-assembled Monolayers on Microelectrodes for Patterning Biomolecules

Published on: August 25, 2009

A Technique to Functionalize and Self-assemble Macroscopic Nanoparticle-ligand Monolayer Films onto Template-free Substrates
08:09

A Technique to Functionalize and Self-assemble Macroscopic Nanoparticle-ligand Monolayer Films onto Template-free Substrates

Published on: May 9, 2014

  • Regulating the aggregation state of Con A by altering environmental pH.

    • Main Results:

    • Successfully fabricated a versatile mixed SAM platform for specific attachment of sugars or proteins.
    • Quantified the rupture forces of multivalent bonds between Con A and mannose.
    • Estimated the rupture force of a single Con A-mannose bond to be 95+/-10 pN.
    • Demonstrated pH-dependent regulation of Con A aggregation and corresponding changes in rupture forces.

    Conclusions:

    • The developed synthesis strategy and mixed SAM platform enable highly specific, single-molecule bond determination.
    • This approach provides a reliable method for investigating lectin-carbohydrate interactions.
    • The technique is applicable to both carbohydrate arrays and lectin arrays for studying molecular binding events.