Nα-Boc-Nω,Nω'-bis-Z-L-arginine
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Nα-Boc-Nω,Nω'-bis-Z-L-arginine

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Nα-Boc-Nω,Nω'-bis-Z-L-arginine, a synthetic compound with widespread usage in proteomics research, serves as a competent agent for the blocking of trypsin digestion. Its versatility extends beyond this application and is also harnessed in peptide and protein synthesis procedures.

Category
BOC-Amino Acids
Catalog number
BAT-004300
CAS number
51219-19-3
Molecular Formula
C27H34N4O8
Molecular Weight
542.60
Nα-Boc-Nω,Nω'-bis-Z-L-arginine
Size Price Stock Quantity
10 g $299 In stock
100 g $999 In stock
Synonyms
Boc-L-Arg(Z)2-OH; (S)-5-(1,3-Bis((Benzyloxy)Carbonyl)Guanidino)-2-((Tert-Butoxycarbonyl)Amino)Pentanoic Acid
Appearance
White to off-white powder
Purity
≥ 98% (HPLC)
Density
1.24±0.1 g/cm3(Predicted)
Melting Point
137-143 °C
Storage
Store at-20 °C
InChI
InChI=1S/C27H34N4O8/c1-27(2,3)39-26(36)29-21(22(32)33)15-10-16-28-23(30-24(34)37-17-19-11-6-4-7-12-19)31-25(35)38-18-20-13-8-5-9-14-20/h4-9,11-14,21H,10,15-18H2,1-3H3,(H,29,36)(H,32,33)(H2,28,30,31,34,35)/t21-/m0/s1
InChI Key
ZWRJPLNCTNRXPE-NRFANRHFSA-N
Canonical SMILES
CC(C)(C)OC(=O)NC(CCCN=C(NC(=O)OCC1=CC=CC=C1)NC(=O)OCC2=CC=CC=C2)C(=O)O

Nα-Boc-Nω,Nω'-bis-Z-L-arginine, a protected form of arginine extensively utilized in research and pharmaceutical realms, demonstrates a host of critical applications. Below are its key applications articulated with heightened perplexity and burstiness:

Peptide Synthesis: Renowned as a pivotal component in peptide and protein synthesis, Nα-Boc-Nω,Nω'-bis-Z-L-arginine functions as a foundational building block. Its Boc (tert-butyloxycarbonyl) and Z (benzyloxycarbonyl) protective groups meticulously safeguard against inadvertent side reactions, ensuring the production of impeccably pure peptides for both research and therapeutic purposes.

Biochemical Research: Delving into arginine's metabolic and functional intricacies, Nα-Boc-Nω,Nω'-bis-Z-L-arginine empowers biochemical investigations. Its incorporation into experimental frameworks enables researchers to probe arginine's involvement in diverse biological processes spanning nitric oxide synthesis to protein synthesis. This immersive exploration amplifies comprehension of cellular signaling and metabolic orchestration.

Drug Development: A cornerstone in the realm of developing arginine-derived pharmaceuticals, Nα-Boc-Nω,Nω'-bis-Z-L-arginine facilitates the crafting and evaluation of modified arginine analogs with enhanced pharmacological attributes. Leveraging the protective form of this compound, researchers can tailor and assess novel therapeutic agents with heightened efficacy and selectivity, heralding a new era in drug design.

Enzyme Studies: Unveiling the mysteries of enzyme kinetics and mechanisms, Nα-Boc-Nω,Nω'-bis-Z-L-arginine emerges as a pivotal substrate analog for arginine-processing enzymes. This unique characteristic allows for meticulous scrutiny of enzyme activity, substrate preferences, and reaction pathways, culminating in a profound understanding of enzymatic functions. Such profound insights aid in sculpting enzyme modulators ranging from inhibitors to activators with promising therapeutic applications at their core.

1.[Total solid phase synthesis of gamma-subunit of cGMP phosphodiesterase from bovine retina and physicochemical properties of synthetic protein].
Rodionova LN1, Zagranichnyĭ VE, Rodionov IL, Lipkin VM, Ivanov VT. Bioorg Khim. 1997 Dec;23(12):933-48.
The 87-membered polypeptide with the sequence of the gamma subunit of cGMP phosphodiesterase from bovine retina rods (PDE gamma) was synthesized by the solid phase method. Two synthetic approaches, which were based on the Boc/Bzl-strategy, were used; both syntheses were carried out in a continuous-flow reactor with swellographic monitoring. In the first approach, five Arg residues were coupled in the form of Boc-Arg(Z)2-OH and the final cleavage of the peptide from the support was effected by the mixture of CF3SO2SiMe3 and thionisole in trifluoroacetic acid. There resulted a heterogeneous, ornitine-rich, and absolutely inactive peptide material which was insoluble in aqueous alkali. In the second approach, Arg(Tos) and the HF low-high cleavage procedure were used, which resulted in a homogeneous polypeptide (according to HPLC and capillary electrophoresis) that manifested correct molecular mass under ion-spray mass spectrometry and the full functional activity characteristic of the native protein.
2.Studies on lactam formation during coupling procedures of N alpha-N omega-protected arginine derivatives.
Cezari MH1, Juliano L. Pept Res. 1996 Mar-Apr;9(2):88-91.
We evaluated the quantity of delta-lactam generated during the synthesis of arginine-containing dipeptides using Z-Arg(Tos)-OH, Boc-Arg(Tos)-OH, Fmoc-Arg(Boc)2-OH and Fmoc-Arg(Pmc)-OH and assayed several carboxyl-activating procedures for coupling the protected arginines to different amino components. We observed significant amounts of delta-lactam during the synthesis of Z-Arg(Tos)-methyl ester and Z-Arg(Tos)-amide, as well as of Boc-Arg(Tos)-chloromethyl ketone. The mixed anhydride coupling procedure and the di-Boc-protecting guanidino group induced more delta-lactam formation than any other coupling or NG-protection method. The amide, benzyl, 4-(NO2)-benzyl and methyl alpha-carboxyl-protected amino acids generated more delta-lactam than did those protected by tertbutyl or N2H2-Boc. So far it has not been possible to propose a general mechanism for delta-lactam formation or a process that completely abolishes it. Therefore, this side reaction should be considered almost inevitable.
3.Synthesis of different types of dipeptide building units containing N- or C-terminal arginine for the assembly of backbone cyclic peptides.
Schumann C1, Seyfarth L, Greiner G, Reissmann S. J Pept Res. 2000 Jun;55(6):428-35.
Different types of dipeptide building units containing N- or C-terminal arginine were prepared for synthesis of the backbone cyclic analogues of the peptide hormone bradykinin (BK: Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg). For cyclization in the N-terminal sequence N-carboxyalkyl and N-aminoalkyl functionalized dipeptide building units were synthesized. In order to avoid lactam formation during the condensation of the N-terminal arginine to the N-alkylated amino acids at position 2, the guanidino function has to be deprotected. The best results were obtained by coupling Z-Arg(Z)2-OH with TFFH/collidine in DCM. Another dipeptide building unit with an acylated reduced peptide bond containing C-terminal arginine was prepared to synthesize BK-analogues with backbone cyclization in the C-terminus. To achieve complete condensation to the resin and to avoid side reactions during activation of the arginine residue, this dipeptide unit was formed on a hydroxycrotonic acid linker.
4.New tris-alkoxycarbonyl arginine derivatives for peptide synthesis.
Izdebski J1, Gers T, Kunce D, Markowski P. J Pept Sci. 2005 Jan;11(1):60-4.
alpha-Alkoxycarbonyl protected ornithines were treated with N,N'-[Z(2Cl)](2)-S-methylisothiourea and N,N'-[Z(2Br)](2)-S-methylisothiourea, N,N'-Z(2)-S-methylisothiourea and N,N'-Boc(2)-S-methylisothiourea to form N(alpha, omega, omega')-tris-alkoxycarbonyl arginines. Two of them, Boc-Arg-{omega,omega'-[Z(2Br)](2)}-OH and Boc-Arg-{omega,omega'-[Z(2Cl)](2)}-OH, were used for the synthesis of dermorphin fragments containing two or three arginine residues. Examination of the products by HPLC and ESI-MS revealed that the purity of the materials obtained with the use of the new derivatives was higher than that obtained in concurrent syntheses in which Boc-Arg(Tos) was used.
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