1392284-57-9Relevant articles and documents
Bivalent HIV-1 fusion inhibitors based on peptidomimetics
Kobayakawa, Takuya,Ebihara, Kento,Tsuji, Kohei,Kawada, Takuma,Fujino, Masayuki,Honda, Yuzuna,Ohashi, Nami,Murakami, Tsutomu,Tamamura, Hirokazu
, (2020/11/07)
Membrane fusion is a valid target for inhibition of HIV-1 replication. A 34-mer fragment peptide (C34), which is contained in the HIV-1 envelope protein gp41, has significant anti-HIV activity. Previously, a dimeric derivative of C34 linked by a disulfide bridge at its C-terminus was found to have more potent anti-HIV activity than the C34 peptide monomer. To date, several peptidomimetic small inhibitors have been reported, but most have lower potency than peptide derivatives related to C34. In the present study we applied this dimerization concept to these peptidomimetic small inhibitors and designed several bivalent peptidomimetic HIV-1 fusion inhibitors. The importance of the length of linkers crosslinking two peptidomimetic compounds was demonstrated and several potent bivalent inhibitors containing tethered peptidomimetics were produced.
Intermediates Stabilized by Tris(triazolylmethyl)amines in the CuAAC Reaction
Chen, Haoqing,Cai, Chengzhi,Li, Siheng,Ma, Yong,Luozhong, Sijin,Zhu, Zhiling
supporting information, p. 4730 - 4735 (2017/04/13)
Tris(triazolylmethyl)amine ligands (TL) are widely used to accelerate the CuI-catalyzed azide-alkyne cycloaddition (CuAAC) reaction, but its mechanistic role remains unclear. Using electrospray ionization mass spectrometry, we detected for the
