Structural Alterations of Mucins Are Associated with Losses in Functionality.


Journal

Biomacromolecules
ISSN: 1526-4602
Titre abrégé: Biomacromolecules
Pays: United States
ID NLM: 100892849

Informations de publication

Date de publication:
12 04 2021
Historique:
pubmed: 23 3 2021
medline: 6 7 2021
entrez: 22 3 2021
Statut: ppublish

Résumé

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.

Identifiants

pubmed: 33749252
doi: 10.1021/acs.biomac.1c00073
doi:

Substances chimiques

Glycoproteins 0
Hydrogels 0
Mucins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1600-1613

Auteurs

Matthias Marczynski (M)

Department of Mechanical Engineering and Munich School of Bioengineering, Technical University of Munich, Boltzmannstraße 15, 85748 Garching, Germany.
Center for Protein Assemblies, Technical University of Munich, Ernst-Otto-Fischer Str. 8, 85748 Garching, Germany.

Kun Jiang (K)

Division of Glycoscience, Department of Chemistry, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH, Royal Institute of Technology, AlbaNova University Center, 106 91 Stockholm, Sweden.
AIMES - Center for the Advancement of Integrated Medical and Engineering Sciences at Karolinska Institutet and KTH Royal Institute of Technology, 114 28 Stockholm, Sweden.
Department of Neuroscience, Karolinska Institute, 171 77 Stockholm, Sweden.

Matthew Blakeley (M)

Division of Glycoscience, Department of Chemistry, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH, Royal Institute of Technology, AlbaNova University Center, 106 91 Stockholm, Sweden.

Vaibhav Srivastava (V)

Division of Glycoscience, Department of Chemistry, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH, Royal Institute of Technology, AlbaNova University Center, 106 91 Stockholm, Sweden.

Francisco Vilaplana (F)

Division of Glycoscience, Department of Chemistry, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH, Royal Institute of Technology, AlbaNova University Center, 106 91 Stockholm, Sweden.

Thomas Crouzier (T)

Division of Glycoscience, Department of Chemistry, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH, Royal Institute of Technology, AlbaNova University Center, 106 91 Stockholm, Sweden.
AIMES - Center for the Advancement of Integrated Medical and Engineering Sciences at Karolinska Institutet and KTH Royal Institute of Technology, 114 28 Stockholm, Sweden.
Department of Neuroscience, Karolinska Institute, 171 77 Stockholm, Sweden.

Oliver Lieleg (O)

Department of Mechanical Engineering and Munich School of Bioengineering, Technical University of Munich, Boltzmannstraße 15, 85748 Garching, Germany.
Center for Protein Assemblies, Technical University of Munich, Ernst-Otto-Fischer Str. 8, 85748 Garching, Germany.

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Classifications MeSH