(R)-2-[(9-Fluorenylmethoxycarbonyl)amino]-4-bromo-4-pentenoic acid
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(R)-2-[(9-Fluorenylmethoxycarbonyl)amino]-4-bromo-4-pentenoic acid

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Category
Fmoc-Amino Acids
Catalog number
BAT-005353
CAS number
220497-92-7
Molecular Formula
C20H18BrNO4
Molecular Weight
416.27
(R)-2-[(9-Fluorenylmethoxycarbonyl)amino]-4-bromo-4-pentenoic acid
IUPAC Name
(2R)-4-bromo-2-(9H-fluoren-9-ylmethoxycarbonylamino)pent-4-enoic acid
Synonyms
(R)-2-Fmoc-amino-4-bromo-4-pentenoic acid; FMOC-D-2-AMINO-4-BROMO-4-PENTENOIC ACID; Fmoc-(R)-(2-bromoallyl)glycine
Appearance
Yellowish solid
Purity
≥ 98% (HPLC)
Density
1.466 g/cm3
Melting Point
110.5 °C
Boiling Point
598.3 °C at 760 mmHg
Storage
Store at 2-8 °C
InChI
InChI=1S/C20H18BrNO4/c1-12(21)10-18(19(23)24)22-20(25)26-11-17-15-8-4-2-6-13(15)14-7-3-5-9-16(14)17/h2-9,17-18H,1,10-11H2,(H,22,25)(H,23,24)/t18-/m1/s1
InChI Key
BYQROHMHEGJMPD-GOSISDBHSA-N
Canonical SMILES
C=C(CC(C(=O)O)NC(=O)OCC1C2=CC=CC=C2C3=CC=CC=C13)Br
1. Thermally Induced Structural Transition of Peptide Nanofibers into Nanoparticles with Enhanced Fluorescence Properties
Qing Li, Xin Yang, Liwei Zhang, Yuefei Wang, Jia Kong, Wei Qi, Yaoyu Liang, Rongxin Su, Zhimin He Chempluschem. 2020 Jul;85(7):1523-1528. doi: 10.1002/cplu.202000116.
A heating treatment method for the synthesis of fluorescent nanoparticles using simple N-(9-fluorenylmethoxycarbonyl) (Fmoc)-protected tripeptides is reported. Two pairs of Fmoc-protected tripeptides (Fmoc-FR1 R2 , R1 =F or W, R2 =H or Y) were designed by changing the amino acid sequences of the peptides. The peptides can self-assemble into nanofibers at lower temperatures, which will spontaneously transform into fluorescent nanoparticles under heating treatment. Moreover, the fluorescence properties of the self-assembled structures can be affected by changing amino acids in the middle of the tripeptide. Specifically, tryptophan (W) can promote fluorescence of the assemblies incubated at high temperatures. Thus, the temperatures and amino sequences of the Fmoc-protected tripeptides have significant effects on the fluorescence of the assembled nanostructures. The results provide a design principle for self-assembled fluorescent peptide nanostructures with potential biomedical applications.
2. Introducing chemical functionality in Fmoc-peptide gels for cell culture
Vineetha Jayawarna, Stephen M Richardson, Andrew R Hirst, Nigel W Hodson, Alberto Saiani, Julie E Gough, Rein V Ulijn Acta Biomater. 2009 Mar;5(3):934-43. doi: 10.1016/j.actbio.2009.01.006. Epub 2009 Jan 18.
Aromatic short peptide derivatives, i.e. peptides modified with aromatic groups such as 9-fluorenylmethoxycarbonyl (Fmoc), can self-assemble into self-supporting hydrogels. These hydrogels have some similarities to extracellular matrices due to their high hydration, relative stiffness and nanofibrous architecture. We previously demonstrated that Fmoc-diphenylalanine (Fmoc-F(2)) provides a suitable matrix for two-dimensional (2D) or three-dimensional (3D) culture of primary bovine chondrocytes. In this paper we investigate whether the introduction of chemical functionality, such as NH(2), COOH or OH, enhances compatibility with different cell types. A series of hydrogel compositions consisting of combinations of Fmoc-F(2) and n-protected Fmoc amino acids, lysine (K, with side chain R=(CH(2))(4)NH(2)), glutamic acid (D, with side chain R=CH(2)COOH), and serine (S, with side chain R=CH(2)OH) were studied. All compositions produced fibrous scaffolds with fibre diameters in the range of 32-65 nm as assessed by cryo-scanning electron microscopy and atomic force microscopy. Fourier transform infrared spectroscopy analysis suggested that peptide segments adopt a predominantly antiparallel beta-sheet conformation. Oscillatory rheology results show that all four hydrogels have mechanical profiles of soft viscoelastic materials with elastic moduli dependent on the chemical composition, ranging from 502 Pa (Fmoc-F(2)/D) to 21.2 KPa (Fmoc-F(2)). All gels supported the viability of bovine chondrocytes as assessed by a live-dead staining assay. Fmoc-F(2)/S and Fmoc-F(2)/D hydrogels in addition supported viability for human dermal fibroblasts (HDF) while Fmoc-F(2)/S hydrogel was the only gel type that supported viability for all three cell types tested. Fmoc-F(2)/S was therefore investigated further by studying cell proliferation, cytoskeletal organization and histological analysis in 2D culture. In addition, the Fmoc-F(2)/S gel was shown to support retention of cell morphology in 3D culture of bovine chondrocytes. These results demonstrate that introduction of chemical functionality into Fmoc-peptide scaffolds may provide gels with tunable chemical and mechanical properties for in vitro cell culture.
3. Chiral capillary electrophoresis with UV-excited fluorescence detection for the enantioselective analysis of 9-fluorenylmethoxycarbonyl-derivatized amino acids
Amir Prior, Giulia Coliva, Gerhardus J de Jong, Govert W Somsen Anal Bioanal Chem. 2018 Aug;410(20):4979-4990. doi: 10.1007/s00216-018-1148-x. Epub 2018 May 29.
The potential of capillary electrophoresis (CE) with ultraviolet (UV)-excited fluorescence detection for sensitive chiral analysis of amino acids (AAs) was investigated. DL-AAs were derivatized with 9-fluorenylmethoxycarbonyl chloride (FMOC)-Cl to allow their fluorescence detection and enhance enantioseparation. Fluorescence detection was achieved employing optical fibers, leading UV excitation light (< 300 nm) from a Xe-Hg lamp to the capillary window, and fluorescence emission to a spectrograph equipped with a charge-coupled device (CCD). Signal averaging over time and emission wavelength intervals was carried out to improve the signal-to-noise ratio of the FMOC-AAs. A background electrolyte (BGE) of 40 mM sodium tetraborate (pH 9.5), containing 15% isopropanol (v/v), 30 mM sodium dodecyl sulfate (SDS), and 30 mM β-cyclodextrin (β-CD), was found optimal for AA chemo- and enantioseparation. Enantioresolutions of 1.0 or higher were achieved for 16 proteinogenic DL-AAs. Limits of detection (LODs) were in the 10-100-nM range (injected concentration) for the D-AA enantiomers, except for FMOC-D-tryptophan (536 nM) which showed intramolecular fluorescence quenching. Linearity (R2 > 0.997) and repeatability for peak height (relative standard deviations (RSDs) < 7.0%; n = 5) and electrophoretic mobility (RSDs < 0.6%; n = 5) of individual AA enantiomers were established for chiral analysis of DL-AA mixtures. The applicability of the method was investigated by the analysis of cerebrospinal fluid (CSF). Next to L-AAs, endogenous levels of D-glutamine and D-aspartic acid could be measured in CSF revealing enantiomeric ratios of 0.35 and 19.6%, respectively. This indicates the method's potential for the analysis of low concentrations of D-AAs in presence of abundant L-AAs.
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