Evaluation of surface charge shift of collagen fibrils exposed to glutaraldehyde

Patrick Mesquida, Dominik Kohl, Orestis Andriotis, Philipp Thurner, Melinda J. Duer, Sneha Bansode, Georg Schitter

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Abstract

Collagen fibrils are a major component of the extracellular matrix. They form nanometer-scale “cables” acting as a scaffold for cells in animal tissues and are widely used in tissue-engineering. Besides controlling their structure and mechanical properties, it is crucial to have information of their surface charge, as this affects how cells attach to the scaffold. Here, we employed Kelvin-probe Force Microscopy to determine the electrostatic surface potential at the single-fibril level and investigated how glutaraldehyde, a well-established protein cross-linking agent, shifts the surface charge to more negative values without disrupting the fibrils themselves. This shift can be interpreted as the result
of the reaction between the carbonyl groups of glutaraldehyde and the amine groups of collagen. It reduces the overall density of positively charged amine groups on the collagen fibril surface and, ultimately, results in the observed negative shift of the surface potential measured. Reactions between
carbonyl-containing compounds and proteins are considered the first step in glycation, the nonenzymatic reaction between sugars and proteins. It is conceivable that similar charge shifts happen in vivo caused by sugars, which could have serious implications on age-related diseases such as diabetes
and which has been hypothesised for many years.
Original languageEnglish
Article number10126
Pages (from-to)1-7
JournalScientific Reports
Volume8
Issue number1
Early online date4 Jul 2018
DOIs
Publication statusPublished - Jul 2018

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