Synthesis and Prpoperties of Ferritin Model Peptides.
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Accession number;02A0304373
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| Title;Synthesis and Prpoperties of Ferritin Model Peptides. |
| Author;
OKU HIROYUKI
(Gunma Univ., Faculty of Engineering)
ARAI KAZUHIKO
(Gunma Univ., Faculty of Engineering)
OSHITA TATSUYA
(Gunma Univ., Faculty of Engineering)
YAMADA KEIICHI
(Gunma Univ., Faculty of Engineering)
KATAKAI RYOICHI
(Gunma Univ., Faculty of Engineering)
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Journal Title;Abstracts. Symposium on Biofunctional Chemistry
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Journal Code:L0836A
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ISSN:
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VOL.16th;NO.;PAGE.34-35(2001)
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| Figure&Table&Reference; |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;Ferritin is an iron storing protein that contains up to 4500 Fe atoms in its protein shell. The protein shell has a symmetrical shape assembled from 24 subunits. It is proposed that the Fe(II) enters via inter-subunit channels located along threefold symmetry axes. In this study, to test the property as a metal ion guide, we have prepared a helical model peptide, t-BuCO-Leu-Leu-Aib-Asp(OBzl)-Phe-Leu-Glu(OBzl)-Ser(Bzl)-(Leu-Leu-Aib)2-OEt (1) has been synthesized. The metal binding property of 1 was studied by CD, UV, 1H NMR, and ESI mass spectra. Our model study suggests that the channel sequence, -Asp-Phe-Leu-Glu-Ser, binds CO2. and Fe2+ ions with a stoichiometry of 0.25-0.50 per peptide, and does not show Fe(II) oxidizing property. (author abst.) |
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