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Updated: Jan 7, 2026

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

ネイティブの高マンノース糖鎖を模倣する調整可能な多価Fe(II)ベースのグリコアセンブリ

Emerson Hall¹, Yu-Shien Sung², Chad W Priest²

¹Department of Biochemistry and Molecular Biophysics, University of California San Diego, La Jolla CA.

bioRxiv : the preprint server for biology

|December 25, 2025

Abstract:

High Mannose Glycans (HMGs) play key roles in eukaryotic biology, regulating processes ranging from protein folding to host pathogen defense. Lectins have evolved to interact with these glycans through multivalent interactions facilitated by the multiple sugars displayed on glycans and via multiple binding sites on each lectin. Using Fe(II) iminopyridine complexes, we generated chemically defined multivalent glycan displays where the valency, arm length, and spatial display of mannose residues can be controlled via subcomponent synthesis. Due to its sensitivity towards the geometric display of mannose residues, monomeric Griffithsin (mGRFT) was utilized as a model lectin. Interactions between the Fe(II) glycan assemblies and mGRFT were characterized using biolayer interferometry (BLI), isothermal titration calorimetry (ITC), and NMR spectroscopy. Our results display a >1000-fold range in K_D for Fe(II) iminopyridine complexes that can be tuned by factors such as saccharide tether length and number of sugars displayed. Through leveraging systematic molecular-level modifications, we demonstrate that tunable Fe(II) glycan assemblies can be used both as mimetics for high mannose glycans as well as competitive inhibitors for native glycan binding.

キーワード:

Fe(II)錯体グリコアセンブリ高マンノース糖鎖レクチン糖鎖模倣多価相互作用結合親和性バイオレイヤー干渉法等温滴定熱量測定

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