Study on Biomaterials for Drug Delivery Sysytem Based on Dynamic Structural Change of Molecular Assembly of Elastin Peptides

点击翻译按钮获取中文摘要

<1995>A high polymer based on the repeating pentapeptide sequence Val-Pro-Gly-Val-Gly which has the property of salf-assembly, a peptide Arg-Gly-Tyr-Ser-Leu-Gly which can be phosphorylated by protein kinase, and two peptides Gly-Ser-Asn-His-Gly and Gly-Arg-Asn-Thr-Gly in which Asn residue can be converted to Asp residue, were synthesized. Arg-Gly-Tyr-Ser-Leu-Gly was phosphorylated by cyclic AMP dpendent protein kinase. The half-lives for Asn-Asp conversion were 6 days and 28 days for Gly-Ser-Asn-His-Gly and Gly-Arg-Asn-Thr-Gly.<1996>Poly [15 (Val-Pro-Gly-Val-Gly), (Arg-Gly-Tyr-Ser-Leu-Gly)] which consists of the indicated molar ratios was synthesized. This polymer was phosphorylated by cyclic AMP dependent protein kinase for 24 hr at 30ﾟC.The resulting phosphorylated polymer poly [15 (Val-Pro-Gly-Val-Gly), (Arg-Gly-Tyr-Ser (PO_4^<2->) -Leu-Gly)] was studied for self-assembly. The temperature for the inverse temperature transition (Tm) of the phosphorylated polymer was shifted to higher temperature giving a shift of 14ﾟC.The phosphorylated polymer was incubated with alkaline phosphatase for 4 hr at 30ﾟC to yield a dephosphorylated poly [15 (Val-Pro-Gly-Val-Gly), (Arg-Gly-Tyr-Ser-Leu-Gly)]. Tm was shifted to lower temperature giving a shift of 13ﾟC.This result indicated complete dephosphorylation of phosphorylated polymer.