| Literature DB >> 33749252 |
Matthias Marczynski1,2, Kun Jiang3,4,5, Matthew Blakeley3, Vaibhav Srivastava3, Francisco Vilaplana3, Thomas Crouzier3,4,5, Oliver Lieleg1,2.
Abstract
Commercial mucin glycoproteins are routinely used as a model to investigate the broad range of important functions mucins fulfill in our bodies, including lubrication, protection against hostile germs, and the accommodation of a healthy microbiome. Moreover, purified mucins are increasingly selected as building blocks for multifunctional materials, i.e., as components of hydrogels or coatings. By performing a detailed side-by-side comparison of commercially available and lab-purified variants of porcine gastric mucins, we decipher key molecular motifs that are crucial for mucin functionality. As two main structural features, we identify the hydrophobic termini and the hydrophilic glycosylation pattern of the mucin glycoprotein; moreover, we describe how alterations in those structural motifs affect the different properties of mucins-on both microscopic and macroscopic levels. This study provides a detailed understanding of how distinct functionalities of gastric mucins are established, and it highlights the need for high-quality mucins-for both basic research and the development of mucin-based medical products.Entities:
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Year: 2021 PMID: 33749252 DOI: 10.1021/acs.biomac.1c00073
Source DB: PubMed Journal: Biomacromolecules ISSN: 1525-7797 Impact factor: 6.988