Abstract
Type I collagen is a major structural protein in mammals that shows highly structured macromolecular organizations specific to each tissue. This biopolymer is synthesized as a triple helix, which self-assembles into fibrils (diameter: 10-300 nm) and further forms various three-dimensional organizations. In recent years, Second Harmonic Generation (SHG) microscopy has emerged as a powerful technique for in situ investigation of the fibrillar collagen structures in biological tissues. However, as an optical technique with typically 300 nm lateral resolution, SHG microscopy cannot resolve most of the collagen fibrils. Moreover, in contrast to incoherent fluorescence signals that scale linearly with the chromophore concentration, SHG is a coherent multiphoton signal that scales quadratically with the density of collagen triple helices aligned in a parallel way in the focal volume. Consequently, quantitative SHG measurements have been limited so far to the averaging of phenomenological parameters [1].
© 2015 IEEE
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