Nα-Fmoc-Nω-bis-carbobenzoxy-L-arginine
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Nα-Fmoc-Nω-bis-carbobenzoxy-L-arginine

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Category
Fmoc-Amino Acids
Catalog number
BAT-007739
CAS number
207857-35-0
Molecular Formula
C37H36N4O8
Molecular Weight
664.72
Nα-Fmoc-Nω-bis-carbobenzoxy-L-arginine
IUPAC Name
(2S)-5-[bis(phenylmethoxycarbonylamino)methylideneamino]-2-(9H-fluoren-9-ylmethoxycarbonylamino)pentanoic acid
Synonyms
Fmoc-L-Arg(Z)2-OH; Fmoc-Arg(Z)2-OH; (9-Fluorenylmethoxycarbonyl)-Ngamma-bis-carbobenzoxy-L-arginine; (S)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-5-((3,7-dioxo-1,9-diphenyl-2,8-dioxa-4,6-diazanonan-5-ylidene)amino)pentanoic acid; (2S)-5-[bis(phenylmethoxycarbonylamino)methylideneamino]-2-(9H-fluoren-9-ylmethoxycarbonylamino)pentanoic acid; (2S)-5-[(di{[(benzyloxy)carbonyl]amino}methylidene)amino]-2-({[(9H-fluoren-9-yl)methoxy]carbonyl}amino)pentanoic acid
Appearance
White to off-white powder
Purity
≥ 98% (HPLC)
Storage
Store at 2-8 °C
InChI
InChI=1S/C37H36N4O8/c42-33(43)32(39-35(44)49-24-31-29-18-9-7-16-27(29)28-17-8-10-19-30(28)31)20-11-21-38-34(40-36(45)47-22-25-12-3-1-4-13-25)41-37(46)48-23-26-14-5-2-6-15-26/h1-10,12-19,31-32H,11,20-24H2,(H,39,44)(H,42,43)(H2,38,40,41,45,46)/t32-/m0/s1
InChI Key
SLWMVWWEOHTNTR-YTTGMZPUSA-N
Canonical SMILES
C1=CC=C(C=C1)COC(=O)NC(=NCCCC(C(=O)O)NC(=O)OCC2C3=CC=CC=C3C4=CC=CC=C24)NC(=O)OCC5=CC=CC=C5

Nα-Fmoc-Nω-bis-carbobenzoxy-L-arginine, a specialized chemical reagent crucial for peptide synthesis and biochemical research, finds diverse applications in scientific endeavors. Here are the key applications:

Peptide Synthesis: Renowned for its role as a protected arginine derivative in solid-phase peptide synthesis, Nα-Fmoc-Nω-bis-carbobenzoxy-L-arginine plays a pivotal role in ensuring the purity and precision of the final peptide product. By safeguarding against unwanted side reactions during synthesis, this compound is indispensable for generating intricate peptides tailored for both research and therapeutic purposes.

Protein Engineering: In the realm of protein engineering, researchers harness the power of Nα-Fmoc-Nω-bis-carbobenzoxy-L-arginine to strategically introduce arginine residues at specific positions within protein sequences. This strategic maneuver allows for a meticulous exploration of arginine’s impact on protein structure, stability, and functionality, offering crucial insights for designing proteins with bespoke properties and functions.

Biochemical Assays: Delving into the world of biochemical assays, this reagent shines in studies involving arginine residues, unraveling mysteries surrounding enzyme activities, protein-protein interactions, and other biochemical phenomena. By incorporating Nα-Fmoc-Nω-bis-carbobenzoxy-L-arginine into assay systems, scientists deepen their comprehension of molecular biology and biochemistry.

Drug Development: In the pharmaceutical arena, Nα-Fmoc-Nω-bis-carbobenzoxy-L-arginine emerges as a linchpin during the evolution of peptide-based drugs. Its role in the accurate synthesis of arginine-containing peptides is paramount, facilitating the creation of potential therapeutic candidates. This precision is critical in the development of treatments targeting diverse diseases, from infectious ailments to cancer.

1.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.
2.A 'conovenomic' analysis of the milked venom from the mollusk-hunting cone snail Conus textile--the pharmacological importance of post-translational modifications.
Bergeron ZL1, Chun JB, Baker MR, Sandall DW, Peigneur S, Yu PY, Thapa P, Milisen JW, Tytgat J, Livett BG, Bingham JP. 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.
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