N-α-(9-Fluorenylmethoxycarbonyl)-3-carbamoyl-L-phenylalanine
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N-α-(9-Fluorenylmethoxycarbonyl)-3-carbamoyl-L-phenylalanine

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Category
Fmoc-Amino Acids
Catalog number
BAT-005408
CAS number
959573-22-9
Molecular Formula
C25H22N2O5
Molecular Weight
430.46
N-α-(9-Fluorenylmethoxycarbonyl)-3-carbamoyl-L-phenylalanine
IUPAC Name
(2S)-3-(3-carbamoylphenyl)-2-(9H-fluoren-9-ylmethoxycarbonylamino)propanoic acid
Synonyms
Fmoc-Phe(3-CONH2)-OH; Fmoc-Phe(3-Carbamoyl)-OH; L-Phenylalanine,3-(aminocarbonyl)-N-[(9H-fluoren-9-ylmethoxy)carbonyl]-; N-α-(9-Fluorenylmethoxycarbonyl)-3-carbamoy-L-phenylalanine; Fmoc-L-3-carbamoylphenylalanine; Fmoc-(2S)-2-amino-3-(3-carbamoylphenyl)propanoic acid
Appearance
White to off-white powder
Purity
≥ 99% (Chiral HPLC)
Density
1.336±0.060 g/cm3 (20 °C, 760 mmHg)
Boiling Point
703.0±60.0 °C at 760 mmHg
Storage
Store at 2-8 °C
InChI
InChI=1S/C25H22N2O5/c26-23(28)16-7-5-6-15(12-16)13-22(24(29)30)27-25(31)32-14-21-19-10-3-1-8-17(19)18-9-2-4-11-20(18)21/h1-12,21-22H,13-14H2,(H2,26,28)(H,27,31)(H,29,30)/t22-/m0/s1
InChI Key
YOTDQRFXBNPJQA-QFIPXVFZSA-N
Canonical SMILES
C1=CC=C2C(=C1)C(C3=CC=CC=C32)COC(=O)NC(CC4=CC(=CC=C4)C(=O)N)C(=O)O
1. A 'conovenomic' analysis of the milked venom from the mollusk-hunting cone snail Conus textile--the pharmacological importance of post-translational modifications
Zachary L Bergeron, et al. Peptides. 2013 Nov;49:145-58. doi: 10.1016/j.peptides.2013.09.004. Epub 2013 Sep 18.
Cone snail venoms provide a largely untapped source of novel peptide drug leads. To enhance the discovery phase, a detailed comparative proteomic analysis was undertaken on milked venom from the mollusk-hunting cone snail, Conus textile, from three different geographic locations (Hawai'i, American Samoa and Australia's Great Barrier Reef). A novel milked venom conopeptide rich in post-translational modifications was discovered, characterized and named α-conotoxin TxIC. We assign this conopeptide to the 4/7 α-conotoxin family based on the peptide's sequence homology and cDNA pre-propeptide alignment. Pharmacologically, α-conotoxin TxIC demonstrates minimal activity on human acetylcholine receptor models (100 μM, <5% inhibition), compared to its high paralytic potency in invertebrates, PD50 = 34.2 nMol kg(-1). The non-post-translationally modified form, [Pro](2,8)[Glu](16)α-conotoxin TxIC, demonstrates differential selectivity for the α3β2 isoform of the nicotinic acetylcholine receptor with maximal inhibition of 96% and an observed IC50 of 5.4 ± 0.5 μM. Interestingly its comparative PD50 (3.6 μMol kg(-1)) in invertebrates was ~100 fold more than that of the native peptide. Differentiating α-conotoxin TxIC from other α-conotoxins is the high degree of post-translational modification (44% of residues). This includes the incorporation of γ-carboxyglutamic acid, two moieties of 4-trans hydroxyproline, two disulfide bond linkages, and C-terminal amidation. These findings expand upon the known chemical diversity of α-conotoxins and illustrate a potential driver of toxin phyla-selectivity within Conus.
2. Preparation of protected peptidyl thioester intermediates for native chemical ligation by Nalpha-9-fluorenylmethoxycarbonyl (Fmoc) chemistry: considerations of side-chain and backbone anchoring strategies, and compatible protection for N-terminal cysteine
C M Gross, D Lelièvre, C K Woodward, G Barany J Pept Res. 2005 Mar;65(3):395-410. doi: 10.1111/j.1399-3011.2005.00241.x.
Native chemical ligation has proven to be a powerful method for the synthesis of small proteins and the semisynthesis of larger ones. The essential synthetic intermediates, which are C-terminal peptide thioesters, cannot survive the repetitive piperidine deprotection steps of N(alpha)-9-fluorenylmethoxycarbonyl (Fmoc) chemistry. Therefore, peptide scientists who prefer to not use N(alpha)-t-butyloxycarbonyl (Boc) chemistry need to adopt more esoteric strategies and tactics in order to integrate ligation approaches with Fmoc chemistry. In the present work, side-chain and backbone anchoring strategies have been used to prepare the required suitably (partially) protected and/or activated peptide intermediates spanning the length of bovine pancreatic trypsin inhibitor (BPTI). Three separate strategies for managing the critical N-terminal cysteine residue have been developed: (i) incorporation of N(alpha)-9-fluorenylmethoxycarbonyl-S-(N-methyl-N-phenylcarbamoyl)sulfenylcysteine [Fmoc-Cys(Snm)-OH], allowing creation of an otherwise fully protected resin-bound intermediate with N-terminal free Cys; (ii) incorporation of N(alpha)-9-fluorenylmethoxycarbonyl-S-triphenylmethylcysteine [Fmoc-Cys(Trt)-OH], generating a stable Fmoc-Cys(H)-peptide upon acidolytic cleavage; and (iii) incorporation of N(alpha)-t-butyloxycarbonyl-S-fluorenylmethylcysteine [Boc-Cys(Fm)-OH], generating a stable H-Cys(Fm)-peptide upon cleavage. In separate stages of these strategies, thioesters are established at the C-termini by selective deprotection and coupling steps carried out while peptides remain bound to the supports. Pilot native chemical ligations were pursued directly on-resin, as well as in solution after cleavage/purification.
3. Syntheses of T(N) building blocks Nalpha-(9-fluorenylmethoxycarbonyl)-O-(3,4,6-tri-O-acetyl-2-azido-2-deoxy-alpha-D-galactopyranosyl)-L-serine/L-threonine pentafluorophenyl esters: comparison of protocols and elucidation of side reactions
Mian Liu, Victor G Young Jr, Sachin Lohani, David Live, George Barany Carbohydr Res. 2005 May 23;340(7):1273-85. doi: 10.1016/j.carres.2005.02.029.
T(N) antigen building blocks Nalpha-(9-fluorenylmethoxycarbonyl)-O-(3,4,6-tri-O-acetyl-2-azido-2-deoxy-alpha-D-galactopyranosyl)-L-serine/L-threonine pentafluorophenyl ester [Fmoc-L-Ser/L-Thr(Ac3-alpha-D-GalN3)-OPfp, 13/14] have been synthesized by two different routes, which have been compared. Overall isolated yields [three or four chemical steps, and minimal intermediary purification steps] of enantiopure 13 and 14 were 5-18% and 6-10%, respectively, based on 3,4,6-tri-O-acetyl-D-galactal (1). A byproduct of the initial azidonitration reaction of the synthetic sequence, that is, N-acetyl-3,4,6-tri-O-acetyl-2-azido-2-deoxy-alpha-D-galactopyranosylamine (5), has been characterized by X-ray crystallography, and shown by 1H NMR spectroscopy to form complexes with lithium bromide, lithium iodide, or sodium iodide in acetonitrile-d3. Intermediates 3,4,6-tri-O-acetyl-2-azido-2-deoxy-alpha-D-galactopyranosyl bromide (6) and 3,4,6-tri-O-acetyl-2-azido-2-deoxy-beta-D-galactopyranosyl chloride (7) were used to glycosylate Nalpha-(9-fluorenylmethoxycarbonyl)-L-serine/L-threonine pentafluorophenyl esters [Fmoc-L-Ser/L-Thr-OPfp, 11/12]. Previously undescribed low-level dehydration side reactions were observed at this stage; the unwanted byproducts were easily removed by column chromatography.
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