Hiring in life sciences? Share your open positions with our professional community. Read more Close

Advertisement

Structure-defined polysaccharide fragments in carbohydrate-protein recognition: Determinants, representative systems, and evidence standards.

Created on 13 Aug 2026

Authors

Lijuan Shi, Shaojie Zhang

Published in

Carbohydrate polymers. Volume 389. Pages 125661. Oct 01, 2026. Epub Jul 18, 2026.

Abstract

Structure-defined carbohydrate entities provide tractable models for determining how heterogeneous polysaccharides engage proteins, but the mechanistic resolution achieved varies widely among polymer classes. This review assesses evidence from heparin/heparan sulfate, pectins, β-glucans, chitin/chitosan, hyaluronan, and marine sulfated glycans. We distinguish partially defined fractions, size- or charge-defined fractions, domain-defined fragments, sequence-defined oligosaccharides, and engineered glycan presentations, and relate each category to the claims it can support. Across representative systems, recognition depends on target-specific combinations of chain length, primary structure and domain architecture, covalent modification and charge pattern, conformation and hydration, and multivalent presentation. Three priorities emerge: generating matched fragment series with structural controls; excluding contamination, aggregation, and assay-format artifacts while accounting for avidity; and confirming binding with complementary assays before establishing target-dependent function. We organize this evidence into a framework that distinguishes fragment-associated activity, structure-correlated effects, direct binding, target necessity, and in vivo causality, while retaining systems-level routes for microbiota- and biomaterial-mediated mechanisms. Aligning claim strength with structural resolution and causal evidence should improve reproducibility and interpretation across carbohydrate-protein recognition studies.

PMID:
42586687
Bibliographic data and abstract were imported from PubMed on 13 Aug 2026.

Read full publication at:
Please sign in to see all details.

Advertisement

Stats

  • Community rating n/a 0 votes
  • Reviewers' rating n/a 0 votes
  • Your rating

1-terrible, 9-excellent. How would you rate this publication? Sign in in to submit your rating.

  • Recommendations n/a n/a positive of 0 vote(s)
  • Views 15
  • Comments 0

Recommended by

  • No recommendations yet.

Post a comment

You need to be signed in to post comments. You can sign in here.

Comments

There are no comments yet.

Advertisement