104091-09-0Relevant articles and documents
Fmoc-OPhth, the reagent of Fmoc protection
Yoshino, Ryo,Tokairin, Yoshinori,Kikuchi, Mari,Konno, Hiroyuki
, p. 1600 - 1603 (2017)
Fmoc-OSu has been widely used for Fmoc protection of amino groups, especially amino acids, in solid phase peptide synthesis. However, it has been recognized that Fmoc-βAla-OH is formed as a by-product via the Lossen rearrangement during the reaction. Since we reconfirmed the formation of Fmoc-βAla-OH during the preparation of Fmoc-AA-OH by Fmoc-OSu, Fmoc-OPhth was designed and synthesized as a new Fmoc reagent to avoid the formation of Fmoc-βAla-OH. Furthermore, Fmoc protection by Fmoc-OPhth and Fmoc-SPPS were evaluated. The various Fmoc-amino acids prepared by Fmoc-OPhth were carried out in good yields and these are applicable in Fmoc-SPPS.
Liquid-chromatography quantitative analysis of 20 amino acids after derivatization with FMOC-CI and its application to different origin Radix isatidis
Zhou, Wei,Zhang, Xiao-Yan,Duan, Geng-Li
, p. 509 - 515 (2011)
We developed a simple, rapid and reliable method for determination of 20 common amino acids based on derivatization with 9-fluorenylmethyl chloroformate (FMOC-CI) and RP-LC/UV, this method was first introduced into quantitative analysis of amino acids. The amino groups of amino acids were trapped with FMOC-CI to form amino acid-FMOC-Cl adducts which can be suitable for LC-UV. Chromatographic separation was performed on a C18 column with a mobile phase gradient consisting of acetonitrile and sodium acetate solution. This method was shown to be sensitive for 20 common amino acids. In the intra-day precisions assay, the range of RSDs was 3.21-7.67% with accuracies of 92.34-102.51%; for the inter-day precisions assay, the range of RSDs was 5.82-9.19% with accuracies of 90.25-100.63%. The results also indicated that solutions of amino acids-FMOC-Cl can be kept at room temperature for at least 24 h without showing significant losses in the quantified values. The validated method was successfully applied to the determination of major four kinds of amino acids in R. isatidis samples (Arg, Pro, Met and Val). The total content of amino acids in different origin R. isatidis was 13.32-19.16 mg/g. The differences between R. isatidis samples were large using HCA.
Conjugate (MTC-220) of muramyl dipeptide analogue and paclitaxel prevents both tumor growth and metastasis in mice
Ma, Yao,Zhao, Nan,Liu, Gang
, p. 2767 - 2777 (2011)
1 (MTC-220), a conjugate of paclitaxel and a muramyl dipeptide analogue, has been synthesized as a novel agent of dual antitumor growth and metastasis activities. In vitro and in vivo tests show that 1 retains its ability to inhibit tumor growth. It is su
Multicomponent hydrogels from enantiomeric amino acid derivatives: Helical nanofibers, handedness and self-sorting
Adhikari, Bimalendu,Nanda, Jayanta,Banerjee, Arindam
, p. 8913 - 8922 (2011)
In this study, chiral helical nanofibers have been obtained from suitable, co-assembling, two oppositely charged amino acid based two component hydrogels. An equimolar mixture of an N-terminally protected amino acid Fmoc-(l/d)Glu (Fmoc: N-fluorenyl-9-methoxycarbonyl, Glu: glutamic acid) and (l/d)Lys (Lys: lysine) can co-assemble to form hydrogels. These hydrogels have been characterised using circular dichroism (CD), atomic force microscopy (AFM), transmission electron microscopy (TEM), X-ray powder diffraction, fluorescence spectroscopic and rheological studies. CD and AFM studies have been extensively used to examine the chiral/achiral nature of fibers obtained from different hydrogel systems. The equimolar mixture of two l-isomers, {Fmoc-(l)Glu + (l)Lys} in the assembled state, leads to the exclusive formation of left-handed helical nanofibers, whereas an equimolar mixture of two d-isomers, {Fmoc-(d)Glu + (d)Lys}, gives rise to right-handed helical nanofibers. The CD study of the gel obtained from the {Fmoc-(l)Glu + (l)Lys} system is exactly the mirror image of the CD signal obtained from the gel of the {Fmoc-(d)Glu + (d)Lys} system. These results suggest that the molecular chirality is being translated into the supramolecular helicity and the handedness of these fibers depends on the corresponding molecular chirality in the mixture of the two component system. Reversing the handedness of helical fibers is possible by using enantiomeric building blocks. Co-assembly of racemic and equimolar mixtures of all four components, i.e., [{Fmoc-(l)Glu + (l)Lys} + {Fmoc-(d)Glu + (d)Lys}] can also form hydrogels. Interestingly, in this racemic mixture self-sorting has been observed with the presence of almost equal amount of left- and right-handed helical nanofibers. The equimolar mixture of Fmoc-(l)Glu and l-ornithine/l-arginine also produces hydrogel with left-handed helical fibers. Moreover, the straight fiber has been observed from the two component hydrogel {Fmoc-(l)Glu + (l)Lys} system in the presence of Ca2+/Mg2+ ions. This indicates the straight nanofibers are obtained under suitable conditions and acid-base interaction is responsible for making the helical fibers at the nanoscale.
SUPRAMOLECULAR GEL SUPPORTED ON OPEN-CELL POLYMER FOAM
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Page/Page column 16-17, (2021/03/19)
The present invention relates to a polymer foam, said polymer foam comprising pores forming an open-cell polymer foam, said polymer foam comprising a supramolecular gel inside pores, and said polymer foam comprising at least one enzyme. The present invention relates to a supramolecular gel; its preparation and its applications, notably in chemical synthesis and kinetic resolution, in particular of organic compounds. The present invention also relates to flow chemistry.
Supported Catalytically Active Supramolecular Hydrogels for Continuous Flow Chemistry
Rodon Fores, Jennifer,Criado-Gonzalez, Miryam,Chaumont, Alain,Carvalho, Alain,Blanck, Christian,Schmutz, Marc,Serra, Christophe A.,Boulmedais,Schaaf, Pierre,Jierry, Lo?c
supporting information, p. 18817 - 18822 (2019/11/16)
Inspired by biology, one current goal in supramolecular chemistry is to control the emergence of new functionalities arising from the self-assembly of molecules. In particular, some peptides can self-assemble and generate exceptionally catalytically active fibrous networks able to underpin hydrogels. Unfortunately, the mechanical fragility of these materials is incompatible with process developments, relaying this exciting field to academic curiosity. Here, we show that this drawback can be circumvented by enzyme-assisted self-assembly of peptides initiated at the walls of a supporting porous material. We applied this strategy to grow an esterase-like catalytically active supramolecular hydrogel (CASH) in an open-cell polymer foam, filling the whole interior space. Our supported CASH material is highly efficient towards inactivated esters and enables the kinetic resolution of racemates. This hybrid material is robust enough to be used in continuous flow reactors, and is reusable and stable over months.
