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Related Concept Videos

Protein-Drug Binding: Determination Methods01:22

Protein-Drug Binding: Determination Methods

Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...

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Related Experiment Video

Updated: Jun 11, 2026

Identifying Protein-protein Interaction Sites Using Peptide Arrays
07:44

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

An array-based method to identify multivalent inhibitors.

Yalong Zhang1, Qian Li, Luis G Rodriguez

  • 1Chemical Biology Laboratory, National Cancer Institute, 376 Boyles Street, Building 376, Frederick, Maryland 21702, USA.

Journal of the American Chemical Society
|June 30, 2010
PubMed
Summary
This summary is machine-generated.

This study presents a novel glycan array platform to analyze carbohydrate-protein interactions by varying glycan structure and presentation density. The platform efficiently identifies multivalent probes and inhibitors for various lectins, crucial for biological research and therapeutic development.

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Peptide-based Identification of Functional Motifs and their Binding Partners
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Last Updated: Jun 11, 2026

Identifying Protein-protein Interaction Sites Using Peptide Arrays
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Peptide-based Identification of Functional Motifs and their Binding Partners
14:28

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

Area of Science:

  • Biochemistry
  • Glycobiology
  • Chemical Biology

Background:

  • Carbohydrate-protein interactions are vital in biological processes.
  • Multivalent interactions, involving ligand structure and presentation, are key for tight binding.
  • Predicting optimal ligand presentation for carbohydrate-binding proteins is challenging.

Purpose of the Study:

  • To develop a high-throughput glycan array platform for analyzing carbohydrate-protein interactions.
  • To create an array with diverse glycan structures and presentation densities (neoglycoprotein density).
  • To identify multivalent probes and inhibitors for various lectins.

Main Methods:

  • Developed a novel glycan array platform with approximately 600 combinations of glycan structure and presentation.
  • Varied neoglycoprotein density, glycan structure, and glycan density on the array surface.
  • Utilized the array to distinguish different types of multivalent complexes.

Main Results:

  • Successfully tested the array with plant lectins: concanavalin A (conA), Vicia villosa isolectin B4 (VVL-B(4)), and Ricinus communis agglutinin (RCA120).
  • Rapidly identified potent multivalent inhibitors for Pseudomonas aeruginosa lectin I (PA-IL) and mouse macrophage galactose-type lectin (mMGL-2).
  • Demonstrated the platform's ability to identify inhibitors without requiring prior structural information of the target lectin/receptor.

Conclusions:

  • The developed glycan array platform is effective for high-throughput analysis of carbohydrate-protein interactions.
  • This approach enables rapid identification of multivalent probes and inhibitors for lectins.
  • The platform offers a valuable tool for biological research and the development of therapeutic agents targeting carbohydrate-protein interactions.