- Preparation method of N-fluorenylmethoxycarbonyl-gamma-(S-triphenylmethyl-cysteamine)-L-glutamic acid
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The invention provides a preparation method of N-fluorenylmethoxycarbonyl-gamma-(S-triphenylmethyl-cysteamine)-L-glutamic acid. The preparation method mainly solves the technical problems of complexity, long period, high cost, and low yield of an original process, and comprises the following steps: (1) preparing N-fluorenylmethoxycarbonyl-L-glutamic acid; (2) preparing N-fluorenylmethoxycarbonyl-L-glutamic acid-1-benzyl ester; (3) preparing S-triphenylmethyl cysteamine; (4) preparing N-fluorenylmethoxycarbonyl-gamma-(S-triphenylmethyl-cysteamine)-L-glutamic acid-alpha-benzyl ester; and (5) preparing N-fluorenylmethoxycarbonyl-gamma-(S-triphenylmethyl-cysteamine)-L-glutamic acid. The method is rapid, high in yield and simple in separation and purification, and the used solvent is environment-friendly and is suitable for mass production.
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- Total Synthesis of L-156,373 and an oxoPiz Analogue via a Submonomer Approach
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The first chemical synthesis of L-156,373 (1), a potent oxytocin receptor antagonist isolated from Streptomyces silvensis, is reported. Assembly of the unusual d-Piz-l-Piz dipeptide subunit was achieved through a sequential electrophilic amination-acylati
- Elbatrawi, Yassin M.,Kang, Chang Won,Del Valle, Juan R.
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supporting information
p. 2707 - 2710
(2018/05/22)
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- Non-proteinogenic amino acids in the pThr-2 position of a pentamer peptide that confer high binding affinity for the polo box domain (PBD) of polo-like kinase 1 (Plk1)
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We report herein that incorporating long-chain alkylphenyl-containing non-proteinogenic amino acids in place of His at the pT-2 position of the parent polo-like kinase 1 (Plk1) polo box domain (PBD)-binding pentapeptide, PLHSpT (1a) increases affinity. Fo
- Qian, Wen-Jian,Park, Jung-Eun,Lee, Kyung S.,Burke Jr., Terrence R.
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supporting information
p. 7306 - 7308
(2013/02/22)
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- Novel synthesis of cyclic amide-linked analogues of angiotensins II and III
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Cyclic amide-linked angiotensin II (ANGII) analogues have been synthesized by novel strategies, in an attempt to test the ring clustering and the charge relay bioactive conformation recently suggested. These analogues were synthesized by connecting side chain amino and carboxyl groups at positions 1 and 8, 2 and 8, 3 and 8, and 3 and 5, N-terminal amino and C-terminal carboxyl groups at positions 1 and 8, 2 and 8, and 4 and 8, and side chain amino to C-terminal carboxyl group at positions 1 and 8. All these analogues were biologically inactive, except for cyclic [Sar1,Asp3,Lys5]ANGII (analogue 10) which had high contractile activity in the rat uterus assay (30% of ANGII) and [Lys1,Tyr(Me)4,Glu8]ANGII (analogue 7) which had weak antagonist activity (PA2 ? 6). Precyclic linear peptides synthesized using 2-chlorotrityl chloride resin and N(α)-Fmoc-amino acids with suitable side chain protection were obtained in high yield and purity and were readily cyclized with benzotriazol-1-yloxytris(dimethylamino)-phosphonium hexafluorophosphate as coupling reagent. Molecular modeling suggests that the ring structure of the potent analogue can be accommodated in the charge relay conformation proposed for ANGII.
- Matsoukas,Hondrelis,Agelis,Barlos,Gatos,Ganter,Moore,Moore
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p. 2958 - 2969
(2007/10/02)
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