Proposed incorporation of elastin into a collagen fibril (hydrophilic and hydrophobic segments of elastin are not shown). The random coil ends of collagen should signify the suggested interference of elastin with collagen's secondary structure during polymerization. Elastin monomers are thought to bind to collagen through local H-bonds, van-der-Waals bonds and ionic bonds, although the latter is less likely due to the low zeta potential.

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... we discussed two extremes of a collagen-elastin interaction, namely, perpendicular and lateral polymerization. While we expected a mixed state between these two extremes prior to the experiments, it became quickly clear that the experiments favored the lateral state over the perpendicular and mixed state (Figure 8). This was also initially proposed as we had observed a Euler buckling-like behavior of the hybrid gels under heating in earlier experiments [13]. ...

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... was directly demonstrated with the LSM recordings of collagen and collagenelastin gels where the collagen was separately stained over the collagen-elastin and further indirectly, as the addition of elastin did not change the structural metrics pore size, fiber thickness or 2D anisotropy. Although we did not quantify changes in the axial and lateral polymerization rate, a visual inspection of the Videos S1-S4 highlights no changes in this polymerization metric after the elastin addition, i.e., the axial fiber growth still Figure 8. Proposed incorporation of elastin into a collagen fibril (hydrophilic and hydrophobic segments of elastin are not shown). ...