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Glycation changes molecular organization and charge distribution in type I collagen fibrils
Sneha Bansode1, Uliana Bashtanova1, Rui Li1
1Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Scientific Reports
|February 27, 2020
Summary
Ribose-5-phosphate (R5P) glycation disrupts collagen fibril structure and increases negative surface charge. This impacts cell adhesion and migration in the tumor microenvironment.
Area of Science:
- Biochemistry
- Cell Biology
- Biomaterials Science
Background:
- Collagen fibrils are key components of the extracellular matrix (ECM), influencing the cellular microenvironment.
- Glycation of collagen affects cell adhesion, migration, and interactions with other ECM components, particularly in cancer.
- Ribose-5-phosphate (R5P) glycation is relevant to the microenvironment of actively dividing cells, including cancer cells.
Purpose of the Study:
- To investigate the structural and surface charge alterations of collagen fibrils upon R5P glycation.
- To understand the implications of these changes on cell adhesion and migration within the tumor microenvironment.
Main Methods:
- Transmission Electron Microscopy (TEM) to observe structural changes in collagen fibrils.
- Kelvin Force Microscopy (KFM) and Fluorescence Lifetime Imaging Microscopy (FLiM) to analyze surface charge properties.
Main Results:
- R5P glycation disrupts the longitudinal molecular ordering within collagen fibrils.
- R5P-glycated collagen fibrils exhibit a more negative surface charge compared to unglycated fibrils.
- Altered molecular arrangement and surface charge are expected to affect cell adhesion site accessibility and ECM integrity.
Conclusions:
- R5P glycation significantly modifies collagen fibril structure and surface charge.
- These modifications have profound implications for cell behavior, including adhesion and migration, within the tumor microenvironment.
- Understanding these glycation effects is crucial for developing targeted cancer therapies.
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