Exploring glycoform-dependent dynamic modulations in human immunoglobulin G via computational and experimental approaches.

ABSTRACT: We investigate the impact of glycoform alterations on the dynamic structure of the human immunoglobulin G1 (IgG1) Fc region using integrated computational and experimental approaches. Four distinct IgG1-Fc glycoforms, varying in core fucosylation and nonreducing terminal galactosylation, were generated through a combination of cell engineering and in vitro enzymatic reactions. Stable-isotope-assisted NMR spectroscopy, incorporating both glycan and protein signals, revealed that galactosylation induces chemical shift perturbations extending from the glycan-protein interface to the C_H2-C_H3 domain boundary. Molecular dynamics simulations demonstrated that the absence of galactose enhances the mobility of both the glycan and the C_H2 domain, broadening the confo

SUBMITTER: Yanaka S 

PROVIDER: S-EPMC12358871 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature