CAS: 51077-16-8; Boc-Thz-Oh

该化合物是一种属于硫化物衍生物类别的手性化合物,其特点是存在硫化物环和碳酸功能组."N-Boc"的标识表明,该矿组受到一个三丁基碳酸(Boc)基(Boc)组的保护,该组通常用于有机合成,以在各种反应中保护胺.该化合物在医药化学中的潜在应用,特别是在药品研制中,值得注意,因为它能够作为较复杂的分子的建筑块.硫化物环有助于其结构的僵硬性,并能够影响其生物活动.此外,该碳酸组的存在还允许其进一步功能化和再活性,使其成为合成路径的多用途中间体.在药物开发方面,其气态(R配置)非常重要,因为立体化学能可以极大地影响由此产生的化合物的药性特性.

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CAS号24424-99-5 二碳酸二叔丁酯 | CAS号34592-47-7 L-硫代脯氨酸 | CAS号444-27-9 噻莫西酸 | CAS号50-00-0 甲醛 | CAS号52-90-4 L-半胱氨酸 | CAS号34592-47-7 L-硫代脯氨酸

合成工艺路线路线简述

    📜L-硫代脯氨酸 反应生成 N-Boc-(R)-噻唑-4-羧酸
    参考文献:Matsui,Takashi;Nagano,Mitsuo;Kitamura,Koichi;Shimizu,Fusaaki
    标题:Matsui,Takashi;Nagano,Mitsuo;Kitamura,Koichi;Shimizu,Fusaaki

    海关参考信息

    专利信息


    专利号:WO-2024165450-A1
    优先权日:2023-02-09
    标题:Method of chemical synthesis of single-chain antibody fragments and products thereby obtained
    发明人:FIGINI MARIANGELA; LUISON ELENA
    权利人:GLYTECH INC; FIGINI MARIANGELA
    摘要:A new method is disclosed for the protein full-chemical synthesis of single-chain antibody fragments (scFv); the obtained products are structurally close and functionally equivalent to their biological counterpart, being however, advantageously free of impurities and more reproducible in properties. The method includes the general steps of: (a) separately synthetizing sub-sequences (peptide fragments) (b) sequentially assembling the sub-sequences obtained in step (a) in the order as they appear in the target scFv amino acid sequence, and (c) performing oxidative folding of the assembled whole peptide molecule obtained in step (b) and dialyzing the resulting product in a buffer.

    专利号:WO-03070764-A1
    优先权日:2002-02-19
    标题:Method for producing interferon
    发明人:STRONG ANDREW EDWARD
    权利人:RMF DICTAGENE SA; STRONG ANDREW EDWARD
    摘要:The invention relates to a method for the chemical synthesis of interferon proteins containing one or more cysteine residues, by the native chemical ligation of segments of the full length interferon protein. The segments of the protein are selected based on the position of the cysteine residues in the interferon protein, with the position of the cysteine residue as a potential site of native chemical ligation. The full-length, fully deprotected polypeptide is folded into biologically active interferon protein by oxidation of the cysteine residues. The invention further relates to the production of the individual peptide fragments which act as intermediates in the synthesis of interferon-alpha. The present invention still further relates to groups of such peptide intermediates which can be utilized together to produce interferon-alpha and interferon-alpha-like proteins.

    专利号:US-7662914-B2
    优先权日:2001-06-05
    标 题 :Native chemical ligation with three or more components
    发明人:VILLAIN MATTEO; GAERTNER HUBERT
    权利人:AMYLIN PHARMACEUTICALS INC
    摘要:The invention provides a method of assembling oligopeptide intermediates in a native chemical ligation reaction that eliminates self-ligation of bi-functional intermediates. An important aspect of the invention is a bi-functional intermediate with an N-terminal cyclic thiazolidine protecting group which effectively prevents self-ligation in the chemical assembly process. The present invention is useful in methods for convergent synthesis of polypeptides and proteins and improves the efficiency of native chemical ligation reactions, particularly where three or more peptide fragments are used to assemble a polypeptide or protein product.

    专利号:WO-2011151826-A2
    优先权日:2010-06-01
    标题:An expeditious synthesis of ubiquitinated peptide conjugates

    专利号:EP-4414386-A1
    优先权日:2023-02-09
    标题 :Method of chemical synthesis of single-chain antibody fragments and products thereby obtained

    专利号:EP-2575849-A2
    优先权日:2010-06-01
    标 题:An expeditious synthesis of ubiquitinated peptide conjugates

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    📌 第三方产品分析报告

    ✅ COA系统入驻 | 共享模式

    合成参考文献


    参考文献:10.1007/s11172-023-4015-7
    摘要:Elisseev IA, Nurieva EV, Zefirov NA, Kolchanova AY, Skvortsov DA, Milaeva ER, Zefirova ON. New C(4)-esters of podophyllotoxin and epipodophyllotoxin with heterocyclic moieties. Russ Chem Bull. 2023 Sep;72(9):2191–6. doi: 10.1007/s11172-023-4015-7.
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