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The recently described in vitro association between elastin or elastin solubilized peptides (ESP) and type I + III collagens has been previously proved by scanning and transmission electron microscopy and by histological studies. The use of a UV-spectroscopic method corroborates the identity of the reaction and enable us to be more precise about its mechanism. The collagen-ESP association is characterized by a 224 nm peak absorbance; the kinetic at this wavelength shows the same three characteristic phases as observed by turbidimetry curves for collagen fibrillogenesis. Spectroscopic studies concerning the effect of Ca 2+ on the reaction reveal that its presence decreases the lag phase and increases the speed of the growth phase; without Ca 2+, collagen can self-react but with a smaller amplitude. Our investigations confirm that, when present, ESP plays a conclusive role in collagen organization.

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