Tools for Structural Lectinomics: From Structures to Lectomes

BBA Advances, Journal Year: 2025, Volume and Issue: unknown, P. 100154 - 100154

Published: March 1, 2025

Lectins are ubiquitous proteins that interact with glycans in a variety of molecular processes and as such, also play role diseases, whether infectious, chronic or cancer-related. The systematic study lectins is therefore essential, particular for understanding cell-cell communication. Accumulated protein three-dimensional structural data the past decades boosted advance AI-based prediction opened up new options to characterise known often be multimeric multivalent. This article reviews methods obtain structures lectins, current available lectin 3D their interactions, how this knowledge used classify these shows combination an array bioinformatics tools should make binding specificity possible near future.

Language: Английский

Controlling Glycan Folding with Ionic Functional Groups

Journal of the American Chemical Society, Journal Year: 2025, Volume and Issue: unknown

Published: April 24, 2025

Glycans are intrinsically flexible molecules that can adopt many conformations. These often carry ionic functional groups influence glycan's conformational preferences, dynamics, and aggregation tendencies. Inspired by these mechanisms, we have engineered a glycan sequence whose secondary structure be precisely manipulated using groups. We strategically incorporated substituents into adopting hairpin conformation. Complementary stabilized the closed conformers, while repulsions shifted populations toward open forms. External stimuli, such as pH variations or enzyme addition, enabled us to dynamically control hairpin's opening closing. Additionally, changes in protonation states led aggregation, suggesting opportunities for creation of responsive glycan-based materials.

Language: Английский

The synergy of experimental and computational approaches for visualizing glycoprotein dynamics: Exploring order within the apparent disorder of glycan conformational ensembles

Current Opinion in Structural Biology, Journal Year: 2025, Volume and Issue: 92, P. 103049 - 103049

Published: April 29, 2025

Understanding the dynamic behavior of glycoproteins is crucial for deciphering their biological roles. This review explores synergistic use experimental and computational methods to address this complex challenge. Glycans, with inherent flexibility structural diversity, pose significant obstacles traditional analysis. Innovative techniques offer valuable snapshots glycan conformations, but often lack context a physiological environment. Computational simulations provide atomic-level detail explore full range motions, require extensive resources validation. Integrating these approaches, by using data refine validate models, essential accurately capturing interplay between glycans proteins. combined strategy promises unlock deeper understanding glycoprotein function inform design novel therapeutics.

Language: Английский