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Mirror Image Mucins and Thio Mucins with Tunable Biodegradation
Victoria R Kohout1, Casia L Wardzala1, Jessica R Kramer1
1Department of Biomedical Engineering, University of Utah, Salt Lake City, Utah 84112, United States.
Journal of the American Chemical Society
|July 20, 2023
Summary
Chemically defined mucin analogues with native glycans were synthesized. This breakthrough offers tunable proteolysis and potential for developing artificial mucins in biomedical applications.
Area of Science:
- Biochemistry
- Glycobiology
- Biomaterials Science
Background:
- Mucin glycoproteins are key components of mucus and the cellular glycocalyx.
- Mucins have critical roles in physiological and pathological processes.
- Current mucin applications are limited by structural heterogeneity and protease susceptibility.
Purpose of the Study:
- To synthesize and characterize chemically defined mucin analogues with native glycans.
- To investigate methods for achieving tunable proteolysis in mucin mimetics.
- To explore the potential of these analogues for biomedical applications.
Main Methods:
- Synthesis of mucin analogues using enantiomer amino acids and glycan thioether linkages.
- Evaluation of proteolysis resistance and cytocompatibility.
- Structural characterization, including analysis of glycoprotein conformation.
Main Results:
- Successful synthesis of chemically defined mucin analogues bearing native glycans.
- Demonstration of tunable proteolysis while maintaining cytocompatibility and binding activity.
- Discovery of a novel mirror-image helix structure, providing insights into glycoprotein conformation.
Conclusions:
- Developed artificial mucins with controlled properties for biomedical use.
- Overcame challenges of structural heterogeneity and protease degradation in mucin applications.
- Paved the way for advanced biomaterials with therapeutic potential.
