Nα,ε-Bis-Z-L-lysine N-hydroxysuccinimide ester
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Nα,ε-Bis-Z-L-lysine N-hydroxysuccinimide ester

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

Category
CBZ-Amino Acids
Catalog number
BAT-003204
CAS number
21160-83-8
Molecular Formula
C26H29N3O8
Molecular Weight
511.53
Nα,ε-Bis-Z-L-lysine N-hydroxysuccinimide ester
IUPAC Name
(2,5-dioxopyrrolidin-1-yl) (2S)-2,6-bis(phenylmethoxycarbonylamino)hexanoate
Synonyms
Z-L-Lys(Z)-OSu; Z-LYSINE(Z)-OSU; Z-LYL(Z)-OSU; Z-LYS-OSU; Bis-N,N'-(Cbz)-L-lysine N-N-hydroxysuccinimide; Z-L-LYSINE N-HYDROXYSUCCINIMIDE ESTER
Appearance
White to off-white powder
Purity
≥ 98% (HPLC)
Density
1.33±0.1 g/cm3
Melting Point
105-115 °C
Storage
Store at 2-8 °C
InChI
InChI=1S/C26H29N3O8/c30-22-14-15-23(31)29(22)37-24(32)21(28-26(34)36-18-20-11-5-2-6-12-20)13-7-8-16-27-25(33)35-17-19-9-3-1-4-10-19/h1-6,9-12,21H,7-8,13-18H2,(H,27,33)(H,28,34)/t21-/m0/s1
InChI Key
LHOAUCZIIQFZMI-NRFANRHFSA-N
Canonical SMILES
C1CC(=O)N(C1=O)OC(=O)C(CCCCNC(=O)OCC2=CC=CC=C2)NC(=O)OCC3=CC=CC=C3
1. Metal-chelating plastic MALDI (pMALDI) chips for the enhancement of phosphorylated-peptide/protein signals
Alfredo J Ibañez, Alexander Muck, Ales Svatos J Proteome Res. 2007 Sep;6(9):3842-8. doi: 10.1021/pr070243r. Epub 2007 Jul 27.
A disposable polymeric pMALDI array with a universal metal cation-chelatable surface for pretreatment/signal enhancement of phosphoproteins and/or phosphopeptides in complex samples was developed. Acrylic acid N-hydroxysuccinimide ester and methyl methacrylate monomers were copolymerized in thin layer molds in a 1:13.3 molar ratio and subsequently treated with Nalpha,Nalpha-bis(carboxymethyl)-l-lysine to obtain a structured planar MALDI array. The prepared NTA pMALDI chip array was activated with metal cations (e.g., Ga(III), Ni(II)), and the selectivities for phosphopeptides (e.g., trypsin-digested alpha-casein (alpha-Cas), and phospho-angiotensin II (p-Ang)) were evaluated using MALDI-TOF/MS. The highest selectivity for proteins was observed for the Ni(II)-NTA chip. The p-Ang was enriched in the presence of BSA tryptic peptides ca. 5 times and represented the major peak after sample adsorption/washing on Ga(III)-NTA chip. The performance of the Ga(III)-chip, tested on alpha-Cas tryptic digest, is fully comparable to commercial systems. Additionally, higher MW peptides and limited methionine oxidation were observed with the chip. A combination of selective absorption of phosphoproteins on Ni(II)-chips and the further enrichment of digested phosphopeptides on the Ga(III)-chip can prove to be very useful for fast identification of unknown proteins using MALDI-TOF/MS.
2. D-Amino acid peptide residualizing agents bearing N-hydroxysuccinimido- and maleimido-functional groups and their application for trastuzumab radioiodination
Marek Pruszynski, Eftychia Koumarianou, Ganesan Vaidyanathan, Satish Chitneni, Michael R Zalutsky Nucl Med Biol. 2015 Jan;42(1):19-27. doi: 10.1016/j.nucmedbio.2014.08.007. Epub 2014 Aug 13.
Introduction: Proteins that undergo receptor-mediated endocytosis are subject to lysosomal degradation, requiring radioiodination methods that minimize loss of radioactivity from tumor cells after this process occurs. To accomplish this, we developed the residualizing radioiodination agent N(ϵ)-(3-[(*)I]iodobenzoyl)-Lys(5)-N(α)-maleimido-Gly(1)-D-GEEEK (Mal-D-GEEEK-[(*)I]IB), which enhanced tumor uptake but also increased kidney activity and necessitates generation of sulfhydryl moieties on the protein. The purpose of the current study was to synthesize and evaluate a new D-amino acid based agent that might avoid these potential problems. Methods: N(α)-(3-iodobenzoyl)-(5-succinimidyloxycarbonyl)-D-EEEG (NHS-IB-D-EEEG), which contains 3 D-glutamates to provide negative charge and a N-hydroxysuccinimide function to permit conjugation to unmodified proteins, and the corresponding tin precursor were produced by solid phase peptide synthesis and subsequent conjugation with appropriate reagents. Radioiodination of the anti-HER2 antibody trastuzumab using NHS-IB-D-EEEG and Mal-D-GEEEK-IB was compared. Paired-label internalization assays on BT474 breast carcinoma cells and biodistribution studies in athymic mice bearing BT474M1 xenografts were performed to evaluate the two radioiodinated D-peptide trastuzumab conjugates. Results: NHS-[(131)I]IB-D-EEEG was produced in 53.8%±13.4% and conjugated to trastuzumab in 39.5%±7.6% yield. Paired-label internalization assays with trastuzumab-NHS-[(131)I]IB-D-EEEG and trastuzumab-Mal-D-GEEEK-[(125)I]IB demonstrated similar intracellular trapping for both conjugates at 1h ((131)I, 84.4%±6.1%; (125)I, 88.6%±5.2%) through 24h ((131)I, 60.7%±6.8%; (125)I, 64.9%±6.9%). In the biodistribution experiment, tumor uptake peaked at 48 h (trastuzumab-NHS-[(131)I]IB-D-EEEG, 29.8%±3.6%ID/g; trastuzumab-Mal-D-GEEEK-[(125)I]IB, 45.3%±5.3%ID/g) and was significantly higher for (125)I at all time points. In general, normal tissue levels were lower for trastuzumab-NHS-[(131)I]IB-D-EEEG, with the differences being greatest in kidneys ((131)I, 2.2%±0.4%ID/g; (125)I, 16.9%±2.8%ID/g at 144 h). Conclusion: NHS-[(131)I]IB-D-EEEG warrants further evaluation as a residualizing radioiodination agent for labeling internalizing antibodies/fragments, particularly for applications where excessive renal accumulation could be problematic.
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