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Fmoc-Ala-OH-[15N]

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Fmoc-Ala-OH-[15N] is a labelled Fmoc-Ala-OH. Alanine is one of the non-essential amino acids for humans. Alanine is the key compound in glucose-alanine cycle.

Category

Fmoc-Amino Acids

Catalog number

BAT-008165

CAS number

117398-49-9

Molecular Formula

C18H17[15N]O4

Molecular Weight

312.33

IUPAC Name

(2S)-2-(9H-fluoren-9-ylmethoxycarbonyl(15N)amino)propanoic acid

Synonyms

N-(9-Fluorenylmethoxycarbonyl)-L-alanine-15N; Fmoc-Ala-OH (15N); Fmoc-Ala-OH-15N

Related CAS

35661-39-3 (Unlabeled CAS)

Purity

98% by HPLC; 98% atom 15N

Density

1.3±0.1 g/cm3

Melting Point

147-153°C (lit.)

InChI

InChI=1S/C18H17NO4/c1-11(17(20)21)19-18(22)23-10-16-14-8-4-2-6-12(14)13-7-3-5-9-15(13)16/h2-9,11,16H,10H2,1H3,(H,19,22)(H,20,21)/t11-/m0/s1/i19+1

InChI Key

QWXZOFZKSQXPDC-DKOIJTIKSA-N

Canonical SMILES

CC(C(=O)O)NC(=O)OCC1C2=CC=CC=C2C3=CC=CC=C13

Fmoc-Ala-OH-[15N], a nitrogen-labeled amino acid derivative, finds diverse applications in biochemical and biophysical studies. Explore its key applications presented with a high degree of perplexity and burstiness: Protein NMR Studies: Delving into the depths of protein structures and dynamics, Fmoc-Ala-OH-[15N] plays a pivotal role in nuclear magnetic resonance (NMR) spectroscopy. The nitrogen-15 isotope emits a distinctive NMR signal, aiding in pinpointing specific atoms or groups within proteins. This facilitates a granular examination of protein folding, interactions, and conformational fluctuations, enriching our understanding of molecular behavior.

Peptide Synthesis: In the realm of solid-phase peptide synthesis, Fmoc-Ala-OH-[15N] is harnessed to incorporate isotopically labeled peptides. These peptides are essential for mass spectrometry-based proteomics and quantitative analytics. Isotopic labeling enables precise quantification of peptide levels and detection of post-translational modifications, unlocking new dimensions in proteomic research.

Metabolic Labeling Experiments: Unraveling the intricacies of cellular protein dynamics, Fmoc-Ala-OH-[15N] serves as a beacon in metabolic labeling experiments. By tracing the incorporation of nitrogen into cellular proteins, researchers can monitor protein synthesis and turnover using mass spectrometry. This approach offers valuable insights into cellular metabolic pathways, shedding light on protein dynamics and turnover dynamics.

Drug Interaction Studies: Aiding in the exploration of drug-protein interactions, the integration of Fmoc-Ala-OH-[15N] into proteins or peptides facilitates advanced drug interaction studies. Leveraging techniques like NMR and mass spectrometry, the nitrogen-15 label assists in tracking binding sites and unraveling the molecular underpinnings of drug actions. This knowledge is instrumental in guiding drug design and development, paving the way for groundbreaking therapeutic innovations.

1.Sequence-specific DNA alkylation targeting for Kras codon 13 mutation by pyrrole-imidazole polyamide seco-CBI conjugates.

Taylor RD1, Asamitsu S, Takenaka T, Yamamoto M, Hashiya K, Kawamoto Y, Bando T, Nagase H, Sugiyama H. Chemistry. 2014 Jan 27;20(5):1310-7. doi: 10.1002/chem.201303295. Epub 2013 Dec 30.

Hairpin N-methylpyrrole-N-methylimidazole polyamide seco-CBI conjugates 2-6 were designed for synthesis by Fmoc solid-phase synthesis, and their DNA-alkylating activities against the Kras codon 13 mutation were compared by high-resolution denaturing gel electrophoresis with 225 base pair (bp) DNA fragments. Conjugate 5 had high reactivity towards the Kras codon 13 mutation site, with alkylation occurring at the A of the sequence 5'-ACGTCACCA-3' (site 2), including minor 1 bp-mismatch alkylation against wild type 5'-ACGCCACCA-3' (site 3). Conjugate 6, which differs from conjugate 5 by exchanging one Py unit with a β unit, showed high selectivity but only weakly alkylated the A of 5'-ACGTCACCA-3' (site 2). The hairpin polyamide seco-CBI conjugate 5 thus alkylates according to Dervan's pairing rule with the pairing recognition which β/β pair targets T-A and A-T pairs. SPR and a computer-minimized model suggest that 5 binds to the target sequence with high affinity in a hairpin conformation, allowing for efficient DNA alkylation.

2.Assessing the utility of infrared spectroscopy as a structural diagnostic tool for β-sheets in self-assembling aromatic peptide amphiphiles.

Fleming S1, Frederix PW, Ramos Sasselli I, Hunt NT, Ulijn RV, Tuttle T. Langmuir. 2013 Jul 30;29(30):9510-5. doi: 10.1021/la400994v. Epub 2013 Jul 16.

β-Sheets are a commonly found structural motif in self-assembling aromatic peptide amphiphiles, and their characteristic "amide I" infrared (IR) absorption bands are routinely used to support the formation of supramolecular structure. In this paper, we assess the utility of IR spectroscopy as a structural diagnostic tool for this class of self-assembling systems. Using 9-fluorene-methyloxycarbonyl dialanine (Fmoc-AA) and the analogous 9-fluorene-methylcarbonyl dialanine (Fmc-AA) as examples, we show that the origin of the band around 1680-1695 cm(-1) in Fourier transform infrared (FTIR) spectra, which was previously assigned to an antiparallel β-sheet conformation, is in fact absorption of the stacked carbamate group in Fmoc-peptides. IR spectra from (13)C-labeled samples support our conclusions. In addition, DFT frequency calculations on small stacks of aromatic peptides help to rationalize these results in terms of the individual vibrational modes.

3.Facile synthesis of mono- and bis-methylated Fmoc-Dap, -Dab and -Orn amino acids.

Lindahl F1, Hoang HN, Fairlie DP, Cooper MA. Chem Commun (Camb). 2015 Mar 14;51(21):4496-8. doi: 10.1039/c4cc09780g.

A new methodology for the synthesis of side chain mono- or bis-methylated Fmoc-Dap, -Dab and -Orn amino acids was developed by probing the reactivity of commercially available Fmoc amino acids.

4.Synthesis of Mannosylated Lipopeptides with Receptor Targeting Properties.

Sedaghat B, Stephenson RJ, Giddam AK, Eskandari S, Apte SH1, Pattinson DJ1, Doolan DL1, Toth I2. Bioconjug Chem. 2016 Mar 16;27(3):533-48. doi: 10.1021/acs.bioconjchem.5b00547. Epub 2016 Jan 25.

Present on the surface of antigen presenting cells (APCs), the mannose receptor (MR) has long been recognized as a front-line receptor in pathogen recognition. During the past decade many attempts have been made to target this receptor for applications including vaccine and drug development. In the present study, a library of vaccine constructs comprising fluorescently labeled mannosylated lipid-dendrimers that contained the ovalbumin CD4(+) epitope, OVA323-339, as the model peptide antigen were synthesized using fluorenylmethyloxycarbonyl (Fmoc) solid phase peptide synthesis (SPPS). The vaccine constructs were designed with an alanine spacer between the O-linked mannose moieties to investigate the impact of distance between the mannose units on receptor-mediated uptake and/or binding in APCs. Uptake studies performed on F4/80(+) and CD11c(+) cells showed significant uptake and/or binding for lipopeptides containing mannose, and also the lipopeptide without mannose when compared to the control peptides (peptide with no lipid and peptide with no mannose and no lipid).