96865-72-4Relevant academic research and scientific papers
Triple Function of 4-Mercaptophenylacetic Acid Promotes One-Pot Multiple Peptide Ligation
Kamo, Naoki,Hayashi, Gosuke,Okamoto, Akimitsu
, p. 16533 - 16537 (2018)
One-pot multiple peptide ligation is a key technology to improve the efficiency of chemical protein synthesis. One-pot repetitive peptide ligation requires a cycle of three steps: peptide ligation, removal of a protecting group, and inactivation of the deprotection reagent. However, previous strategies are not sufficient because of harsh deprotection conditions, slow deprotection rates, and difficulty in quenching the deprotection reagent. To address these issues, we developed a rapid, efficient deprotection and subsequent quenching strategy using an allyloxycarbonyl group to protect the N-terminal cysteine residue. 4-Mercaptophenylacetic acid (MPAA), a thiol additive for native chemical ligation, functioned not only as a scavenger for π-allyl palladium complexes, but also as a quencher of palladium(0) complexes. By utilizing the multifunctionality of MPAA, we carried out a one-pot five-segment ligation to afford histone H2AX (142 amino acids), which was isolated in 59 % yield.
Diaminodiacid bridge improves enzymatic and in vivo inhibitory activity of peptide CPI-1 against botulinum toxin serotype A
Shen, Jintao,Liu, Jia,Yu, Shuo,Yu, Yunzhou,Huang, Chao,Xiong, Xianghua,Yue, Junjie,Dai, Qiuyun
supporting information, p. 4049 - 4052 (2021/04/19)
The replacement of the disulfide bridge of CPI-1, a peptide inhibitor of light chain of Botulinum toxin serotype A, with the thioether-containing and biscarba-containing diaminodiacid bridge leads to a significant decrease in the degradation by trypsin and increase in the detoxification activity in vivo, the addition of hydrophobic or positive amino acid at C-terminus of modified peptides further improves the inhibitory activity.
Diaminodiacid-based solid-phase synthesis of peptide disulfide bond mimics
Cui, Hong-Kui,Guo, Ye,He, Yao,Wang, Feng-Liang,Chang, Hao-Nan,Wang, Yu-Jia,Wu, Fang-Ming,Tian, Chang-Lin,Liu, Lei
supporting information, p. 9558 - 9562 (2013/09/23)
The antimicrobial peptide tachyplesin I was used as a model to apply the title strategy, which was developed for the preparation of peptidic macrocycles with double disulfide surrogates. The folding and activity of the tachyplesin I analogues were found to be sensitive to the structure of the disulfide surrogates, thus underlining the necessity of a flexible synthetic route for generating disulfide bond surrogates with high structural diversity. Copyright
Synthesis and activity of thioether-containing analogues of the complement inhibitor compstatin
Knerr, Patrick J.,Tzekou, Apostolia,Ricklin, Daniel,Qu, Hongchang,Chen, Hui,Van Der Donk, Wilfred A.,Lambris, John D.
scheme or table, p. 753 - 760 (2012/08/14)
Disulfide bonds are essential for the structural stability and biological activity of many bioactive peptides. However, these bonds are labile to reducing agents, which can limit the therapeutic utility of such peptides. Substitution of a disulfide bond w
Hetero Diels-Alder synthesis of 3-hydroxypyridines: Access to the nosiheptide core
Lu, Jin-Yong,Arndt, Hans-Dieter
, p. 4205 - 4212 (2008/02/05)
The 1-azadiene hetero Diels-Alder reaction of silylated enol oximes with alkynes was investigated and was optimized to furnish 2,5,6-trisubstituted 3-hydroxypyridines in high yields in one simple operation. Importantly, monosubstituted alkynyl ketones were found to lead to the formation of the 6-isomer with exceptional regioselectivity (>95:5). This methodology was applied to a scaleable synthesis of the core structure of the potent antibiotic nosiheptide. Protecting groups were optimized, which led to a racemization-free seven-step synthesis of the key building block.
