75957-53-8Relevant academic research and scientific papers
Sequential Intermolecular Radical Addition and Reductive Radical Cyclization of Tyrosine and Phenylalanine Derivatives with Alkenes via Photoinduced Decarboxylation: Access to Ring-Constrained γ-Amino Acids
Osaka, Kazuyuki,Usami, Ayuka,Iwasaki, Tomoya,Yamawaki, Mugen,Morita, Toshio,Yoshimi, Yasuharu
, p. 9480 - 9488 (2019/07/08)
Sequential radical addition to alkenes and reductive radical cyclization of phenylalanine and tyrosine derivatives via photoinduced decarboxylation furnished ring-constrained γ-amino acids under mild conditions. A variety of alkenes such as acrylamides and acrylic esters could be employed in the photoinduced radical cascade cyclization. The yields of the ring-constrained γ-amino acids are dependent on the electron-accepting ability and steric hindrance of the alkene used. The proposed sequential reaction can also be applied for direct tethering of dipeptides to yield unique ring-constrained tetrapeptides.
Tetrahydro-β-carboline-3-carboxyl-thymopentin: A nano-conjugate for releasing pharmacophores to treat tumor and complications
Hu, Xi,Zhao, Ming,Wang, Yuji,Wang, Yaonan,Zhao, Shurui,Wu, Jianhui,Li, Xiangmin,Peng, Shiqi
, p. 1384 - 1397 (2016/03/05)
To improve the therapeutic efficacy of cancer patients a novel conjugate of thymopentin (TP5) and (1S,3S)-1-methyl-tetrahydro-β-carboline-3-carboxylic acid (MTC) was presented. In water and mouse plasma MTCTP5 forms the nanoparticles of 14-139 nm in diameter, the suitable size for delivery in blood circulation. In mouse plasma MTCTP5 releases MTC, while in the presence of trypsin MTCTP5 releases MTC and TP5. On mouse and rat models the MTCTP5 dose dependently slows down the tumor growth, inhibits inflammatory response and blocks thrombosis. The anti-tumor activity as well as the anti-inflammation activity and anti-thrombotic activity of MTCTP5 are 100 fold and 10 fold higher than those of MTC, respectively, which are attributed to the fact that it down-regulates the plasma levels of TNF-α and IL-8 of the treated animals. The immunology enhancing activities in vitro and in vivo of MTCTP5 are similar to those of TP5, which is attributed to the fact that MTCTP5 up-regulates the plasma levels of IL-2 and CD4 as well as down-regulates the plasma level of CD8 of the treated animals. The plasma alanine transaminase, aspartate transaminase and creatinine assays indicate that MTCTP5 therapy does not injure the liver and the kidney of the animals. The survival time of MTCTP5 treated mice is significantly longer than that of TP5 treated mice.
Conformationally constrained macrocycles that mimic tripeptide β-strands in water and aprotic solvents
Reid, Robert C.,Kelso, Michael J.,Scanlon, Martin J.,Fairlie, David P.
, p. 5673 - 5683 (2007/10/03)
The β-strand conformation is unknown for short peptides in aqueous solution, yet it is a fundamental building block in proteins and the crucial recognition motif for proteolytic enzymes that enable formation and turnover of all proteins. To create a gener
Immunoactive peptides: VI. Synthesis of new analogs of thymopoietin
Anokhina,Levushkina,Sorochinskaya
, p. 1339 - 1344 (2007/10/03)
A new scheme for preparing a pentapeptide of thymopoietin (ArgLysAspValTyr, TP-5) is proposed, featuring a versatile combination of the maximal and minimal protection principles. The scheme was used to prepare the Gly2, Pro2, Ala3, and Arg2, Ala3 analogs of TP-5.
PEPTIDE DERIVATIVES AND ANGIOTENSIN IV RECEPTOR AGONIST
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, (2008/06/13)
Short-chain peptide derivatives acting on angiotensin IV receptor at low concentrations. Because of agonistically acting on angiotensin IV receptor, the novel peptide derivatives of the present invention represented by the following formula (1) are useful as remedies for various diseases in which angiotensin IV participates:
A Convenient Synthesis of Thymopentin
Bobde, Vivek,Dasgupta, S.,Chauhan, V. S.
, p. 1124 - 1126 (2007/10/02)
A convenient and economical solution phase synthesis of thymopentin in which the side chain of tyrosine is left unprotected is reported.
