# Probing Glycosaminoglycan–Protein Interactions: Applications of Surface Plasmon Resonance

## TL;DR

This review explores how surface plasmon resonance is used to study interactions between glycosaminoglycans and proteins, highlighting recent advances and challenges in the field.

## Contribution

The paper provides a systematic and up-to-date review of SPR applications in glycosaminoglycan–protein interaction studies.

## Key findings

- SPR offers label-free, real-time insights into GAG–protein binding kinetics and specificity.
- Recent technological advances improve SPR sensitivity and throughput for GAG studies.
- GAG heterogeneity and immobilization remain significant experimental challenges.

## Abstract

Glycosaminoglycans (GAGs) are highly negatively charged polysaccharides that play essential roles in numerous physiological and pathological processes through their interactions with proteins. These interactions govern cellular signaling, inflammation, coagulation, and recognition. Surface Plasmon Resonance (SPR) has emerged as a key biophysical technique for label-free, real-time characterization of biomolecular interactions, offering insights into binding kinetics, affinity, and specificity. SPR-based approaches to glycosaminoglycan–protein interaction studies offer powerful tools for elucidating the roles of GAGs in a wide range of physiological and pathological processes. In this review, we systematically discuss experimental strategies, data analysis methods, and representative applications of SPR-based glycosaminoglycan–protein interactions. Special attention is given to the challenges associated with GAG heterogeneity and immobilization, as well as recent technological advances that enhance sensitivity and throughput. To our knowledge, this review represents one of the first systematic and up-to-date summaries specifically focused on recent advances in applying SPR to the study of glycosaminoglycan–protein interactions.