Impact of Glycoclustering on Stiffening of MUC5AC Peptides Revealed by High-Efficiency Synthesis.

ABSTRACT: Clustered O-glycosylation of long tandem repeat regions is the hallmark of secreted mucins such as MUC5AC. Glycosylation is thought to play a key role in rigidifying the peptide backbone. The synthesis of peptides containing extended O-glycosylation clusters has proven challenging, thus limiting studies on the influence of glycoclustering on peptide structure. Here, we report an efficient glyco-economic synthesis of peptides featuring a previously unattained degree of glycoclustering. The method is based on a fully automated, DMF-free solid-phase synthesis employing the solvent 1,3-dioxolane (DOL) in all steps. The addition of Tween-20 enabled fast couplings of and to GalNAcylated amino acids by using only 0.5 excess equivalents at room temperature. Five tandem repeats long MUC5AC glycopep

SUBMITTER: Galashov A 

PROVIDER: S-EPMC12559463 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature