Studies on Peptides. CLXVIII. : Syntheses of Three Peptides Isolated from Horseshoe Crab Hemocytes, Tachyplesin I, Tachyplesin II, and Polyphemusin I
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- 赤路 健一
- Faculty of Pharmaceutical Sciences, Kyoto University
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- 藤井 信孝
- Faculty of Pharmaceutical Sciences, Kyoto University
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- 徳永 文稔
- Department of Biology, Faculty of Science, Kyushu University
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- 宮田 敏行
- Department of Biology, Faculty of Science, Kyushu University
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- 岩永 貞昭
- Department of Biology, Faculty of Science, Kyushu University
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- 矢島 治明
- Faculty of Pharmaceutical Sciences, Kyoto University
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Tachyplesin I, a 17-residue peptide amide with two disulfide bridges isolated from an acid extract of horseshoe crab hemocyte debris, was synthesized by the 9-fluorenylmethyloxycarbonyl (Fmoc)-based solid-phase method followed by two steps of deprotection and subsequent air-oxidation. The thioanisole-mediated deprotection with 1 M trifluoromethanesulfonic acid was first employed to cleave the peptide amide from the resin and, at the same time, to deprotect the side chain protecting groups employed, except for the S-Acm (acetamidomethyl) group. The 4 Acm groups attached were next cleaved by silver trifluoromethanesulfonate. In addition, two related peptides, tachyplesin II and polyphemusin I, were similarly synthesized. Synthetic tachyplesin I inhibited the lipopolysaccharide-mediated activation of clotting factor C to the same extent as did the corresponding natural peptide. The relative potencies of synthetic tachyplesin II and synthetic polyphemusin I with respect to natural tachyplesin I (taken as 1) were 2.1 and 0.61,respectively.
収録刊行物
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- Chemical & pharmaceutical bulletin
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Chemical & pharmaceutical bulletin 37 (10), 2661-2664, 1989-10-25
公益社団法人日本薬学会
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詳細情報 詳細情報について
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- CRID
- 1573105977299143680
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- NII論文ID
- 110003627300
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- NII書誌ID
- AA00602100
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- ISSN
- 00092363
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- 本文言語コード
- en
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- データソース種別
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- CiNii Articles