Calcium ion binding to carbonyls of elastin hexapeptide

✍ Scribed by D.W. Urry; T. Ohnishi

• Book ID: 104106080
• Publisher: Elsevier Science
• Year: 1974
• Weight: 464 KB
• Volume: 3
• Category: Article
• ISSN: 0006-3061
• DOI: 10.1016/s0006-3061(00)82010-4

✦ Synopsis

Carbon-13 and proton magnetic resonance studies are reported on the interaction of calcium ions with a hexapeptide that is a repeating sequence in elastin . Of the seven carbonyls in N-formyl-L-Val-L-Ala-L-Pro-Gly-L-Val-Gly-OMe, six are observed to titrate downfield on sequential CaC1 : addition . Deshielding of the peptide carbonyl carbon results from cation interaction with the carbonyl moiety. This study provides the first direct evidence of elastin carbonyl binding to calcium ion which has been proposed as the initiating step in the pathological calcification of arterial elastic fibers. A working model for the conformation of the hexapeptide-calcium ion complex is presented .