Age and temperature effects on collagen structure, stability and mechanics

Collagen is the predominant structural protein in humans, representing over 25% of protein mass in our bodies, and fulfilling key mechanical and signalling functions in the extracellular matrix and connective tissues. As we age, collagens gradually acquire nonenzymatic chemical modifications known as Age-related Glycation End-products (AGEs). How these chemical modifications affect the interplay between structure, stability and mechanics of individual collagen proteins is not known. In this study, we combine biochemical approaches with atomic force microscopy (AFM) imaging, to investigate how these properties of collagen are affected by AGEs. We furthermore study how collagen’s thermally induced denaturation at body temperatures can be understood by use of this single-molecule imaging approach. Our results provide insight into how its surrounding environment can influence the function of this important protein.