(2S,3S,4R,5S)-3,4,5-trihydroxy-6,6-bis(phenylthio)hexan-2-yl 4-methylbenzenesulfonate | 1394279-88-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: (2S,3S,4R,5S)-3,4,5-trihydroxy-6,6-bis(phenylthio)hexan-2-yl 4-methylbenzenesulfonate
• CAS: 1394279-88-9
• 化学式: C₂₅H₂₈O₆S₃
• 分子量: 520.692
• InChiKey: GMVQDHXGHSOYJZ-QMTRIVCPSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  None
• 重原子数：
  None
• 可旋转键数：
  None
• 环数：
  None
• sp3杂化的碳原子比例：
  None
• 拓扑面积：
  None
• 氢给体数：
  None
• 氢受体数：
  None

反应信息

• 作为产物：
  描述：

  (2s,3r,4r,5s)-1,1-Bis(phenylthio)hexane-2,3,4,5-tetraol 、 对甲苯磺酰氯 在 吡啶 作用下， 反应 48.0h， 以50%的产率得到(2S,3S,4R,5S)-3,4,5-trihydroxy-6,6-bis(phenylthio)hexan-2-yl 4-methylbenzenesulfonate
  参考文献：
  名称：

  Banuelos-Hernandez; Mendoza-Espinoza, South African Journal of Chemistry, 2012, vol. 65, p. 84 - 90

  摘要：

  DOI：

文献信息

• Bike peptides: a ride through the membrane
  作者：Júlia García-Pindado、Soledad Royo、Meritxell Teixidó、Ernest Giralt

  DOI：10.1002/psc.2993

  日期：2017.4

  Several natural peptides have a biaryl or biaryl ether motif in their biologically active structures. A model bicyclic pentapeptide containing a biaryl bridge has been synthesized by solid‐phase peptide synthesis combining on‐resin Suzuki and Miyaura cross‐coupling reactions. Its biological properties in terms of permeability, stability and cytotoxicity have been studied, demonstrating the positive

  几种天然肽在其生物活性结构中具有联芳基或联芳基醚基序。通过结合树脂铃木和Miyaura交叉偶联反应的固相肽合成法，合成了一个包含联芳基桥的双环五肽模型。已研究了其在通透性，稳定性和细胞毒性方面的生物学特性，证明了联芳桥的积极作用，出色的膜渗透性和血清稳定性。©2017欧洲多肽协会和John Wiley＆Sons，Ltd.
• Discovery of Potent and Orally Bioavailable Macrocyclic Peptide–Peptoid Hybrid CXCR7 Modulators
  作者：Markus Boehm、Kevin Beaumont、Rhys Jones、Amit S. Kalgutkar、Liying Zhang、Karen Atkinson、Guoyun Bai、Janice A. Brown、Heather Eng、Gilles H. Goetz、Brian R. Holder、Bhagyashree Khunte、Sarah Lazzaro、Chris Limberakis、Sangwoo Ryu、Michael J. Shapiro、Laurie Tylaska、Jiangli Yan、Rushia Turner、Siegfried S. F. Leung、Mahesh Ramaseshan、David A. Price、Spiros Liras、Matthew P. Jacobson、David J. Earp、R. Scott Lokey、Alan M. Mathiowetz、Elnaz Menhaji-Klotz

  DOI：10.1021/acs.jmedchem.7b01028

  日期：2017.12.14

  The chemokine receptor CXCR7 is an attractive target for a variety of diseases. While several small-molecule modulators of CXCR7 have been reported, peptidic macro cycles may provide advantages in terms of potency, selectivity, and reduced off-target activity. We produced a series of peptidic macrocycles that incorporate an N-linked peptoid functionality where the peptoid group enabled us to explore side-chain diversity well beyond that of natural amino acids. At the same time, theoretical calculations and experimental assays were used to track and reduce the polarity while closely monitoring the physicochemical properties. This strategy led to the discovery of macrocyclic peptide peptoid hybrids with high CXCR7 binding affinities (K-i < 100 nM) and measurable passive permeability (P-app > S X 10(-6) cm/s). Moreover, bioactive peptide 25 (K-i = 9 nM) achieved oral bioavailability of 18% in rats, which was commensurate with the observed plasma clearance values upon intravenous administration.
• Oostatic peptides containing d-amino acids: synthesis, oostatic activity, degradation, accumulation in ovaries and NMR study
  作者：Jan Hlaváček、Richard Tykva、Josef Holík、Blanka Bennettová、Miloš Buděšínský、Věra Vlasáková、Bohuslav Černý、Jiřina Slaninová

  DOI：10.1007/s00726-011-0882-6

  日期：2012.5

  Analogs of the H-Tyr-Asp-Pro-Ala-Pro-OH pentapeptide with d-amino acid residues either in differing or in all of the positions of the sequences were prepared and their oostatic potency was compared with that of the parent pentapeptide. The d-amino acid residue containing analogs exhibited an equal or even higher oostatic effect in the flesh fly Neobellieria bullata than the parent peptide. Contrary to the rapid incorporation of radioactivity from the labeled H-Tyr-Asp-[H-3]Pro-Ala-Pro-OH pentapeptide into the ovaries of N. bullata in vitro, the radioactivity incorporation from the labeled pentapeptides with either d-aspartic acid or d-alanine was significantly delayed. As compared to the parent pentapeptide, also the degradation of both the d-amino acid-containing analogs mentioned above proceeded at a significantly lower rate. The decreased intake of radioactivity, the lower degradation and finally also the high oostatic effect may be ascribed to the decreased enzymatic degradation of the peptide bonds neighboring the d-amino acid residues in the corresponding peptides. The introduction of the non-coded d-amino acids thus enhances the oostatic effect in N. bullata owing to the prolonged half-life of the corresponding pentapeptides, which can thus affect more ovarian cells.