ArticleScience advances2025
Chemical synthesis uncovers the significant impact of natural glycosylation on islet amyloid polypeptide aggregation.
Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Article
- Site-Specific and Programmable Editing of Serine and Threonine in Unprotected Peptides.Journal of the American Chemical Society · 2026Article
- Deciphering How Clustered O‑Glycosylation Shapes Substrate-Binding Preferences in an Intrinsically Disordered Protein Region.JACS Au · 2026Article
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein and peptide aggregation poses substantial challenges in disease pathology and therapeutic development. While natural glycosylation may mitigate aggregation, its efficacy and underlying mechanisms remain poorly understood due to limited access to homogeneous samples with complex glycans. This study addresses these knowledge gaps by investigating the natural glycosylation of islet amyloid polypeptide (IAPP), a peptide with therapeutic potential for type 2 diabetes but problematic aggregation. An optimized chemical synthesis enabled preparation of diverse IAPP glycoforms with complex glycan structures, allowing systematic evaluation of their effects on aggregation, cytotoxicity, and solubility. Sialylated glycans at Thr
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