Peptide-Mucin Binding and Biosimilar Mucus-Permeating Properties
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Updated: Oct 6, 2025

Mucin Agarose Gel Electrophoresis: Western Blotting for High-molecular-weight Glycoproteins
Published on: June 14, 2016
Xiaohong Sun1,2, Raliat O Abioye3, Ogadimma D Okagu3
1School of Nutrition Sciences, Faculty of Health Sciences, University of Ottawa, Ottawa, ON K1H 8M5, Canada.
Abstract:
This study aimed to understand the role of the mucus layer (a biological hydrogel) in the transport mechanisms of peptides. Using established in vitro models, the mucin-binding activity and mucus-permeating property of peptides were determined. Uncharged peptides with relatively high hydrophilicity, including MANT, TNGQ, and PASL, as well as cationic peptides, including KIPAVF and KMPV, possessed strong mucin-binding activity. Contrarily, uncharged peptides with high hydrophobicity index, including YMSV and QIGLF, exhibited weak mucin-binding activity. Only TNGQ, which has high Boman index and hydrophilicity, showed a high biosimilar mucus-permeating property with a permeability of 96 ± 30% after 60 min. TNGQ showed the potential for high bioavailability due to the high mucin-binding and biosimilar mucus-permeating activities.
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