Cross-linked polypentapeptide of elastin as a calcifiable matrix: molecular weight dependence.

The polypentapeptide, (L X Val1-L X Pro2-Gly3-L X Val4-Gly5)n, when cross-linked by gamma-irradiation was shown to calcify when exposed to dialysates of calcium and phosphate augmented fetal bovine sera and the molecular weight dependence of this calcification is investigated. Five molecular weight fractions, labeled I to V in order of increasing polymer size from under 12,000 dalton (I), that is, n less than 30, to over 100,000 daltons (V), that is, n greater than 240, were gamma-irradiation cross-linked at 10-12 MRAD to form matrices I-V. Calcium-45 was used to follow the time course and relative amount of calcium uptake from the sera. Scanning electron microscopy and electron probe microanalysis were used to characterize the extent of matrix calcification. All matrices took up calcium-45 from the sera; however, only matrices formed from polypentapeptide with n greater than 100 calcified, that is, matrices III, IV, and V. Matrix V with n greater than 240 calcified massively and in a manner comparable to chemically cross-linked polypentapeptide with n approximately 40 using nonaugmented sera. Presumably, gamma-irradiation results in chain breakage. The gamma-irradiation cross-linked matrices with values of n ranging from under 30 to greater than 240 establish the molecular weight dependence of matrix calcification.