Fmoc-Chloride
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Fmoc-Chloride

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Reagent for the introduction of Fmoc-amino-protecting group, which is stable towards acids but is readily cleaved under mildly basic non-hydrolytic conditions.

Category
Peptide Synthesis Reagents
Catalog number
BAT-004867
CAS number
28920-43-6
Molecular Formula
C15H11ClO2
Molecular Weight
258.70
Fmoc-Chloride
IUPAC Name
9H-fluoren-9-ylmethyl carbonochloridate
Synonyms
Fmoc-CL; Chloroformic acid 9-fluorenylmethyl ester; 9-Fluorenylmethyl chloroformate; 1-(9-Fluorenyl)methyl chloroformate; Fluorene-9-methanol, Chloroformate (8CI); 9-Fluorenylmethoxycarbonyl Chloride; 9-Fluorenylmethyl Chlorocarbonate; 9H-Fluoren-9-ylmethyl Chloroformate; AminoTag; FMOC Chloride; Fluorenylmethyl Chloroformate; FmocCl
Appearance
White to yellow crystalline powder
Purity
≥ 98% (HPLC)
Density
1.178 g/cm3 (Predicted)
Melting Point
62-64 °C
Boiling Point
365.8 °C (Predicted)
Storage
-20 °C under inert atmosphere
Solubility
Slightly soluble in Chloroform, Ethyl Acetate
InChI
InChI=1S/C15H11ClO2/c16-15(17)18-9-14-12-7-3-1-5-10(12)11-6-2-4-8-13(11)14/h1-8,14H,9H2
InChI Key
IRXSLJNXXZKURP-UHFFFAOYSA-N
Canonical SMILES
C1=CC=C2C(=C1)C(C3=CC=CC=C32)COC(=O)Cl
1.Amino-acids condensations in the preparation of N alpha-9-fluorenylmethyloxycarbonylamino-acids with 9-fluorenylmethylchloroformate.
Tessier M, Albericio F, Pedroso E, Grandas A, Eritja R, Giralt E, Granier C, Van Rietschoten J. Int J Pept Protein Res. 1983 Jul;22(1):125-8.
Synthesis of N alpha-9-fluorenylmethyloxycarbonyl (Fmoc) amino-acids by reaction of free amino-acids (glycine and alanine) with 9-fluorenylmethylchloroformate leads to formation of small amounts of Fmoc-dipeptide which are difficult to eliminate by crystallization. The alternative way to prepare Fmoc-amino-acids by reacting the Fmoc-chloride first with sodium azide and then with the free amino-acid eliminates this side reaction, at least for glycine and alanine.
2.Determination of atmospheric amines by on-fiber derivatization solid-phase microextraction with 2,3,4,5,6-pentafluorobenzyl chloroformate and 9-fluorenylmethoxycarbonyl chloride.
Parshintsev J1, Rönkkö T2, Helin A2, Hartonen K2, Riekkola ML3. J Chromatogr A. 2015 Jan 9;1376:46-52. doi: 10.1016/j.chroma.2014.12.040. Epub 2014 Dec 18.
Alkylamines play an important role in atmospheric chemistry and are of concern for human health. Determining them from the vapor phase is challenging owing to their high polarity and volatility, water solubility, low concentrations, and poor chromatographic properties. We propose on-fiber derivatization solid-phase microextraction (SPME) to increase sensitivity and selectivity for the determination of alkylamines in air samples. SPME fibers coated in head-space with 2,3,4,5,6-pentafluorobenzyl chloroformate (PFBCF, 10min) or 9-fluorenylmethoxycarbonyl (FMOC) chloride (5min) were exposed to the sample for 5-120min, after which the derivatized alkylamines were thermally desorbed in the GC injection port and analyzed by GC-MS. The specific focus of the research was dimethylamine (DMA) but, as well as secondary amines, both coating agents readily react with primary and tertiary amines and with ammonia at ambient temperatures. The fiber coating procedures, sampling times, and analytical conditions were optimized, and methods were tested with natural samples.
3.Fluorescein-conjugated lysine monomers for solid phase synthesis of fluorescent peptides and PNA oligomers.
Lohse J1, Nielsen PE, Harrit N, Dahl O. Bioconjug Chem. 1997 Jul-Aug;8(4):503-9.
Fluorescein ethyl ester, I, was used to prepare the fluorescent mixed ester/ether 6-O-(carboxymethyl)-fluorescein ethyl ester, III. Conjugation of III to the epsilon-amino group of alpha-N-Boc-L-lysine, via the N-hydroxysuccinimde ester, IV, gave the Boc-protected fluorescein-conjugated lysine monomer V. Removal of the Boc group, followed by reaction with Fmoc chloride, gave the Fmoc-protected monomer, VI (Figure 1). These Boc- and Fmoc-protected fluorescein-conjugated lysines were readily incorporated into peptides and PNA oligomers during solid phase synthesis to give fluorescent products. Mass spectroscopy and UV studies showed that the fluorophore remains unchanged during solid phase synthesis. In contrast to fluorescein, the photophysical properties of these derivatives are pH independent from pH 3 to 8, with a molar absorption coefficient, epsilon max 456, of 2.9 x 10(4) M-1 cm-1 and fluorescence quantum yield, phi f, of 0.18.
4.Influence of gelatin matrices cross-linked with transglutaminase on the properties of an enclosed bioactive material using beta-galactosidase as model system.
Fuchsbauer HL1, Gerber U, Engelmann J, Seeger T, Sinks C, Hecht T. Biomaterials. 1996 Aug;17(15):1481-8.
Transglutaminase (protein-glutamine: amine gamma-glutamyltransferase, EC 2.3.2.13) from Streptoverticillium mobaraense has been used to stabilize immobilisates produced with beta-galactosidase (beta-D-galactoside galactohydrolase, EC 3.2.1.23) from Aspergillus oryzae and acid-processed gelatins of different qualities as support. The isopeptide level of N epsilon-(gamma-L-glutamyl)-L-lysine bonds formed by transglutaminase was determined to estimate their influence on the kinetic properties of the enclosed beta-galactosidase. An HPLC procedure using precolumn derivatization of the gelatin hydrolysates with FMOC-chloride was chosen which permits the analysis of cross-linked lysine with satisfactory precision. Depending on the gelatin quality, the degree of cross-links necessary for the transformation of gelatin into an insoluble protein was in the range 0.3-32.3% of the available lysine residues. beta-Galactosidase was entrapped in the gelatin matrices with a yield of 8-46% of the initial activity.
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