pubmed-article:18613286 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18613286 | lifeskim:mentions | umls-concept:C0025663 | lld:lifeskim |
pubmed-article:18613286 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
pubmed-article:18613286 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
pubmed-article:18613286 | lifeskim:mentions | umls-concept:C1527148 | lld:lifeskim |
pubmed-article:18613286 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
pubmed-article:18613286 | pubmed:issue | 11 | lld:pubmed |
pubmed-article:18613286 | pubmed:dateCreated | 2008-10-27 | lld:pubmed |
pubmed-article:18613286 | pubmed:abstractText | A novel strategy for a more efficient synthesis of difficult sequence-containing peptides, the S-acyl isopeptide method, was developed and successfully applied. A model pentapeptide Ac-Val-Val-Cys-Val-Val-NH2 was synthesized via its water-soluble S-acyl isopeptide using an S-acyl isodipeptide unit, Boc-Cys(Fmoc-Val)-OH. An S-acyl isopeptide possessing excellent water solubility could be readily and quantitatively converted to the native peptide via an S--N intramolecular acyl migration reaction at pH 7.4. Thus, the S-acyl isopeptide method provides a useful tool in peptide chemistry. | lld:pubmed |
pubmed-article:18613286 | pubmed:language | eng | lld:pubmed |
pubmed-article:18613286 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18613286 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18613286 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18613286 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18613286 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18613286 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18613286 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18613286 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18613286 | pubmed:month | Nov | lld:pubmed |
pubmed-article:18613286 | pubmed:issn | 1075-2617 | lld:pubmed |
pubmed-article:18613286 | pubmed:author | pubmed-author:KuoS PSP | lld:pubmed |
pubmed-article:18613286 | pubmed:author | pubmed-author:KimuraTooruT | lld:pubmed |
pubmed-article:18613286 | pubmed:author | pubmed-author:KisoYoshiakiY | lld:pubmed |
pubmed-article:18613286 | pubmed:author | pubmed-author:YoshiyaTakuT | lld:pubmed |
pubmed-article:18613286 | pubmed:copyrightInfo | Copyright (c) 2008 European Peptide Society and John Wiley & Sons, Ltd. | lld:pubmed |
pubmed-article:18613286 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:18613286 | pubmed:volume | 14 | lld:pubmed |
pubmed-article:18613286 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18613286 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18613286 | pubmed:pagination | 1203-8 | lld:pubmed |
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pubmed-article:18613286 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18613286 | pubmed:articleTitle | Isopeptide method: development of S-acyl isopeptide method for the synthesis of difficult sequence-containing peptides. | lld:pubmed |
pubmed-article:18613286 | pubmed:affiliation | Department of Medicinal Chemistry, Division of Medicinal Chemical Sciences, Center for Frontier Research in Medicinal Science, 21st Century COE Program, Kyoto Pharmaceutical University, Yamashina-ku, Kyoto, Japan. | lld:pubmed |
pubmed-article:18613286 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18613286 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |