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Glycation changes molecular organization and charge distribution in type I collagen fibrils.

Scientific reports (2020-02-27)
Sneha Bansode, Uliana Bashtanova, Rui Li, Jonathan Clark, Karin H Müller, Anna Puszkarska, Ieva Goldberga, Holly H Chetwood, David G Reid, Lucy J Colwell, Jeremy N Skepper, Catherine M Shanahan, Georg Schitter, Patrick Mesquida, Melinda J Duer
ABSTRACT

Collagen fibrils are central to the molecular organization of the extracellular matrix (ECM) and to defining the cellular microenvironment. Glycation of collagen fibrils is known to impact on cell adhesion and migration in the context of cancer and in model studies, glycation of collagen molecules has been shown to affect the binding of other ECM components to collagen. Here we use TEM to show that ribose-5-phosphate (R5P) glycation of collagen fibrils - potentially important in the microenvironment of actively dividing cells, such as cancer cells - disrupts the longitudinal ordering of the molecules in collagen fibrils and, using KFM and FLiM, that R5P-glycated collagen fibrils have a more negative surface charge than unglycated fibrils. Altered molecular arrangement can be expected to impact on the accessibility of cell adhesion sites and altered fibril surface charge on the integrity of the extracellular matrix structure surrounding glycated collagen fibrils. Both effects are highly relevant for cell adhesion and migration within the tumour microenvironment.

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Supelco
Amino acid standards, physiological, analytical standard, acidics, neutrals, and basics