Figure 1 | Scientific Reports

Figure 1

From: Determination of extracellular matrix collagen fibril architectures and pathological remodeling by polarization dependent second harmonic microscopy

Figure 1The alternative text for this image may have been generated using AI.

Hierarchical organization of collagen fibrils. (a) Cylindrical organization of peptide bonds β around single helix (H) main axis. Helix angle θH = 53°, pitch PH = 0.95 nm and diameter DH = 0.3 nm. (b) Cylindrical coil-coil of three single helices around triple helix (3helix, 3 H) main axis. 3helix angle \({\theta }_{3H}=12^\circ \), pitch P3H = 8.5 nm and diameter D3H = 0.6 nm. (c) Cylindrical organization of the triple helix around main axis of the supercoiled (SC) fibril. Supercoil angle \({\theta }_{SC}=17^\circ \), pitch PSC = 1 μm and diameter DSC = 100 nm. (d) Bundle of well aligned fibrils with bundle main axis along z direction that is in the plane of the microscope stage (see Fig. 1g). (e) Bundle of well aligned and tilted fibrils along y direction with angle \({\theta }_{Tc}\) with z direction. (f) Bundle of disordered fibrils within a cone with half apex angle \({\theta }_{Tr}\) with z direction. (g) Microscope stage with fixed laboratory coordinates system X, Y, Z. \(\gamma \) and \(\alpha \) are angles between respectively z direction and input polarization with Z direction. Light propagates in y = Y direction. For (a–c), diameters D and pitches P are from references23,24.

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