Unexpected original property of elastin derived proteins: spontaneous tight coupling with natural and synthetic polymers.

Abstract Elastin fibres can be decomposed into their constituting proteins using several processes; in particular by saponification of some bonds with KOH in aqueous tertiobutyl alcohol, elastin solubilized proteins - ESP- of 10 to 200 KDa were produced with a good yield (70–80%). It is demonstrated that some of these proteins were capable of tightly re-associating with the native elastin fibres and remained bound on the fibres, in spite of several drastic washes using 1 M Guanidinium, HCl at 37°C for 1 h. At pH 4–5, approximately 30–40 μg ESP were retained per mg elastin. The same association is also shown to occur, under similar conditions, with Poly-ethylene-terephtalate, Poly-hexamethylene diamine-adipic acid but not with polyurethanes. The optimal conditions of the coupling were described as depending on ESP concentration, time, pH, ionic strength and Ca ++ . It was also shown that opposite pH conditions, i.e. pH 14, 0.5 M NaOH, could allow the retained proteins to desorb from polyesters. Hence, it will be possible to determine the sort of proteins which could be involved. This property of ESP allows us 1. to better understand the exceptional capacity of tissue repair certainly due to adhesive properties of the artificial connective matrices containing elastin or ESP, developed in our laboratory, 2. to provide a new approach for elucidating elastin microstructure and function, 3. especially to provide a new mode for coating certain fibres, yielding materials with bioactive and biofonctional qualities.