Nα-Fmoc-Nβ-Boc-L-2,3-diaminopropionic acid
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Nα-Fmoc-Nβ-Boc-L-2,3-diaminopropionic acid

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Category
BOC-Amino Acids
Catalog number
BAT-005670
CAS number
162558-25-0
Molecular Formula
C23H26N2O6
Molecular Weight
426.46
Nα-Fmoc-Nβ-Boc-L-2,3-diaminopropionic acid
IUPAC Name
(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-[(2-methylpropan-2-yl)oxycarbonylamino]propanoic acid
Synonyms
Fmoc-L-Dap(Boc)-OH
Appearance
White powder
Purity
≥ 98% (HPLC)
Density
1.263 g/cm3
Melting Point
131-139 .°C
Storage
Store at 2-8°C
InChI
InChI=1S/C23H26N2O6/c1-23(2,3)31-21(28)24-12-19(20(26)27)25-22(29)30-13-18-16-10-6-4-8-14(16)15-9-5-7-11-17(15)18/h4-11,18-19H,12-13H2,1-3H3,(H,24,28)(H,25,29)(H,26,27)/t19-/m0/s1
InChI Key
PKAUMAVONPSDRW-IBGZPJMESA-N
Canonical SMILES
CC(C)(C)OC(=O)NCC(C(=O)O)NC(=O)OCC1C2=CC=CC=C2C3=CC=CC=C13
1.Ring size in cyclic endomorphin-2 analogs modulates receptor binding affinity and selectivity.
Piekielna J1, Kluczyk A, Gentilucci L, Cerlesi MC, Calo' G, Tomböly C, Łapiński K, Janecki T, Janecka A. Org Biomol Chem. 2015 Jun 7;13(21):6039-46. doi: 10.1039/c5ob00565e.
The study reports the solid-phase synthesis and biological evaluation of a series of new side chain-to-side chain cyclized opioid peptide analogs of the general structure Tyr-[D-Xaa-Phe-Phe-Asp]NH2, where Xaa = Lys (1), Orn (2), Dab (3), or Dap (4) (Dab = 2,4-diaminobutyric acid, Dap = 2,3-diaminopropionic acid), containing 17- to 14-membered rings. The influence of the ring size on binding to the MOP, DOP and KOP opioid receptors was studied. In general, the reduction of the size of the macrocyclic ring increased the selectivity for the MOP receptor. The cyclopeptide incorporating Xaa = Lys displayed subnanomolar MOP affinity but modest selectivity over the KOP receptor, while the analog with the Orn residue showed increased affinity and selectivity for MOP. The analog with Dab was a weak MOP agonist and did not bind to the other two opioid receptors. Finally, the peptide with Xaa = Dap was completely MOP receptor-selective with subnanomolar affinity.
2.A novel branched TAT(47-57) peptide for selective Ni(2+) introduction into the human fibrosarcoma cell nucleus.
Szyrwiel Ł1, Shimura M, Shirataki J, Matsuyama S, Matsunaga A, Setner B, Szczukowski Ł, Szewczuk Z, Yamauchi K, Malinka W, Chavatte L, Łobinski R. Metallomics. 2015 Jul;7(7):1155-62. doi: 10.1039/c5mt00021a.
A TAT47-57 peptide was modified on the N-terminus by elongation with a 2,3-diaminopropionic acid residue and then by coupling of two histidine residues on its N-atoms. This branched peptide could bind to Ni under physiological conditions as a 1 : 1 complex. We demonstrated that the complex was quantitatively taken up by human fibrosarcoma cells, in contrast to Ni(2+) ions. Ni localization (especially at the nuclei) was confirmed by imaging using both scanning X-ray fluorescence microscopy and Newport Green fluorescence. A competitive assay with Newport Green showed that the latter displaced the peptide ligand from the Ni-complex. Ni(2+) delivered as a complex with the designed peptide induced substantially more DNA damage than when introduced as a free ion. The availability of such a construct opens up the way to investigate the importance of the nucleus as a target for the cytotoxicity, genotoxicity or carcinogenicity of Ni(2+).
3.Deciphering the Substrate Specificity of SbnA, the Enzyme Catalyzing the First Step in Staphyloferrin B Biosynthesis.
Kobylarz MJ1, Grigg JC1, Liu Y1, Lee MS1, Heinrichs DE, Murphy ME1. Biochemistry. 2016 Feb 16;55(6):927-39. doi: 10.1021/acs.biochem.5b01045. Epub 2016 Feb 3.
Staphylococcus aureus assembles the siderophore, staphyloferrin B, from l-2,3-diaminopropionic acid (l-Dap), α-ketoglutarate, and citrate. Recently, SbnA and SbnB were shown to produce l-Dap and α-ketoglutarate from O-phospho-l-serine (OPS) and l-glutamate. SbnA is a pyridoxal 5'-phosphate (PLP)-dependent enzyme with homology to O-acetyl-l-serine sulfhydrylases; however, SbnA utilizes OPS instead of O-acetyl-l-serine (OAS), and l-glutamate serves as a nitrogen donor instead of a sulfide. In this work, we examined how SbnA dictates substrate specificity for OPS and l-glutamate using a combination of X-ray crystallography, enzyme kinetics, and site-directed mutagenesis. Analysis of SbnA crystals incubated with OPS revealed the structure of the PLP-α-aminoacrylate intermediate. Formation of the intermediate induced closure of the active site pocket by narrowing the channel leading to the active site and forming a second substrate binding pocket that likely binds l-glutamate.
4.Synthesis of L-2,3-diaminopropionic acid, a siderophore and antibiotic precursor.
Kobylarz MJ1, Grigg JC1, Takayama SJ1, Rai DK1, Heinrichs DE2, Murphy ME3. Chem Biol. 2014 Mar 20;21(3):379-88. doi: 10.1016/j.chembiol.2013.12.011. Epub 2014 Jan 30.
L-2,3-diaminopropionic acid (L-Dap) is an amino acid that is a precursor of antibiotics and staphyloferrin B a siderophore produced by Staphylococcus aureus. SbnA and SbnB are encoded by the staphyloferrin B biosynthetic gene cluster and are implicated in L-Dap biosynthesis. We demonstrate here that SbnA uses PLP and substrates O-phospho-L-serine and L-glutamate to produce a metabolite N-(1-amino-1-carboxyl-2-ethyl)-glutamic acid (ACEGA). SbnB is shown to use NAD(+) to oxidatively hydrolyze ACEGA to yield α-ketoglutarate and L-Dap. Also, we describe crystal structures of SbnB in complex with NADH and ACEGA as well as with NAD(+) and α-ketoglutarate to reveal the residues required for substrate binding, oxidation, and hydrolysis. SbnA and SbnB contribute to the iron sparing response of S. aureus that enables staphyloferrin B biosynthesis in the absence of an active tricarboxylic acid cycle.
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