Abstract
Synthetic elastin hexapeptides, N-formyl-Val-Ala-Pro-Gly-Val-Gly- O-methyl, n-formyl-Ala-Pro-Gly-Val-Gly-Val- O-methyl, and N-formyl-Pro-Gly-Val-Gly-Val-Ala- O-methyl were studied in order to determine their affinity and selectivity for calcium, magnesium, strontium, sodium, and potassium ions. Of the three permutations N-forrnyl-Val-Ala-Pro-Gly-Val-Gly- O-methyl had the highest calcium affinity, k a ∼- 0.5 × 10 6. All three hexamers displayed a selectivity toward calcium, although strontium did bind well also. The peptides could not compete effectively with water for magnesium ions and had little affinity for sodium and potassium ions. The significance of these results lies in the possible role of this hexameric sequence in calcium binding in natural elastin.
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