Fmoc-L-phenylalanine
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Fmoc-L-phenylalanine

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L-Phenylalanine derivative is used in the preparation of peptides and deltorphin derivatives. A potential inhibitor of IGF-I and IGF-Binding Protein-5 complex.

Category
Fmoc-Amino Acids
Catalog number
BAT-003773
CAS number
35661-40-6
Molecular Formula
C24H21NO4
Molecular Weight
387.40
Fmoc-L-phenylalanine
IUPAC Name
(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-phenylpropanoic acid
Synonyms
Fmoc-L-Phe-OH; N-[(9H-Fluoren-9-ylMethoxy)carbonyl]-L-phenylalanine; N-FMOC-PHE-OH; N-Fmoc-(S)-phenylalanine
Appearance
White to off-white powder
Purity
≥ 99.7% (Chiral HPLC)
Density
1.276 g/cm3
Melting Point
180-187 °C
Boiling Point
513.4 °C
Storage
Store at 2-8 °C
InChI
InChI=1S/C24H21NO4/c26-23(27)22(14-16-8-2-1-3-9-16)25-24(28)29-15-21-19-12-6-4-10-17(19)18-11-5-7-13-20(18)21/h1-13,21-22H,14-15H2,(H,25,28)(H,26,27)/t22-/m0/s1
InChI Key
SJVFAHZPLIXNDH-QFIPXVFZSA-N
Canonical SMILES
C1=CC=C(C=C1)CC(C(=O)O)NC(=O)OCC2C3=CC=CC=C3C4=CC=CC=C24
1. Hybrid supramolecular gels of Fmoc-F/halloysite nanotubes: systems for sustained release of camptothecin
C Rizzo, R Arrigo, F D'Anna, F Di Blasi, N T Dintcheva, G Lazzara, F Parisi, S Riela, G Spinelli, M Massaro J Mater Chem B. 2017 May 7;5(17):3217-3229. doi: 10.1039/c7tb00297a. Epub 2017 Apr 13.
Supramolecular gel hybrids obtained by self-assembly of Fmoc-l-phenylalanine (Fmoc-F) in the presence of functionalized halloysite nanotubes (f-HNT) were obtained in biocompatible solvents and employed as carriers for the delivery of camptothecin (CPT) molecules. The synthesis of the new f-HNT material as well as its characterization are described. The properties of the hybrid hydrogels and organogels were analyzed by several techniques. The presence of small amounts of f-HNT allows good dispersion of the tubes and the subsequent formation of homogeneous gels. The experimental results show that f-HNT functions only as an additive in the hybrid gels and does not demonstrate gelator behavior. The in vitro kinetic release from both f-HNT/CPT and Fmoc-F/f-HNT/CPT was studied in media that imitates physiological conditions, and the factors controlling the release process were determined and discussed. Furthermore, the antiproliferative in vitro activities of the gels were evaluated towards human cervical cancer HeLa cells. A comparison of data collected in both systems shows the synergistic action of f-HNT and the gel matrix in controlling the release of CPT in the media and maintaining the drug in its active form. Finally, a comparison with pristine HNT is also reported. This study suggests a suitable strategy to obtain two-component gel hybrids based on nanocarriers with controlled drug carrier capacity for biomedical applications.
2. Identification of inhibitors of the E. coli chaperone SurA using in silico and in vitro techniques
Eric W Bell, Erica J Zheng, Lisa M Ryno Bioorg Med Chem Lett. 2018 Dec 1;28(22):3540-3548. doi: 10.1016/j.bmcl.2018.09.034. Epub 2018 Sep 29.
SurA is a gram-negative, periplasmic chaperone protein involved in the proper folding of outer membrane porins (OMPs), which protect bacteria against toxins in the extracellular environment by selectively regulating the passage of nutrients into the cell. Previous studies demonstrated that deletion of SurA renders bacteria more sensitive to toxins that compromise the integrity of the outer membrane. Inhibitors of SurA will perturb the folding of OMPs, leading to disruption of the outer membrane barrier and making the cell more vulnerable to toxic insults. The discovery of novel SurA inhibitors is therefore of great importance for developing alternative strategies to overcome antibiotic resistance. Our laboratory has screened over 10,000,000 compoundsin silicoby computationally docking these compounds onto the crystal structure of SurA. Through this screen and a screen of fragment compounds (molecular weight less than 250 g/mol), we found twelve commercially readily available candidate compounds that bind to the putative client binding site of SurA. We confirmed binding to SurA by developing and employing a competitive fluorescence anisotropy-based binding assay. Our results show that one of these compounds, Fmoc-β-(2-quinolyl)-d-alanine, binds the client binding site with high micromolar affinity. Using this compound as a lead, we also discovered that Fmoc-l-tryptophan and Fmoc-l-phenylalanine, but not Fmoc-l-tyrosine, bind SurA with similar micromolar affinity. To our knowledge, this is the first report of a competitive fluorescence anisotropy assay developed for the identification of inhibitors of the chaperone SurA, and the identification of three small molecules that bind SurA at its client binding site.
3. Chiral analysis of biogenic DL-amino acids derivatized by urethane - protected alpha-amino acid N-carboxyanhydride using capillary zone electrophoresis and micellar electrokinetic chromatography
Martin Pumera, Martin Flegel, Ludek Lepsa, Ivan Jelínek Electrophoresis. 2002 Aug;23(15):2449-56. doi: 10.1002/1522-2683(200208)23:153.0.CO;2-X.
A new analytical method for enantioselective separation of DL-amino acids derivatized by N-fluorenylmethoxycarbonyl-L-alanyl N-carboxyanhydride (FMOC-L-Ala-NCA) using capillary electrophoresis was developed. Separation parameters, such as composition and pH of the background electrolyte, and concentration of gamma-cyclodextrin (in capillary zone electrophoresis) and sodium dodecyl sulfate (in micellar electrokinetic chromatography) were optimized. The separation method was validated and it suits well for purity analysis. Detection limit of the method was 0.2% of the minor enantiomer in the major one. The level of racemization in coupling during solid-phase peptide synthesis was studied using capillary electrophoresis with gamma-cyclodextrin as a chiral selector. The anchorage of the first (C-terminal) amino acid derivative to the solid supports bearing the hydroxylic groups is the key step of the synthesis affecting the extent of its racemization. FMOC-L-phenylalanine was chosen as the suitable model amino acid derivative making it possible to study the degree of racemization of N-fluorenylmethoxycarbonyl-L-alanine-L-phenylalanine synthesized on different polymer resins, using the different condensation agents.
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