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

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Category
BOC-Amino Acids
Catalog number
BAT-004522
CAS number
143824-77-5
Molecular Formula
C31H40N4O8
Molecular Weight
596.70
Nα-Fmoc-Nω,Nω'-bis-Boc-L-arginine
IUPAC Name
(2S)-5-[bis[(2-methylpropan-2-yl)oxycarbonylamino]methylideneamino]-2-(9H-fluoren-9-ylmethoxycarbonylamino)pentanoic acid
Synonyms
Fmoc-L-Arg(Boc)2-OH; (S)-5-[[Bis(Boc-Amino)Methylene]Amino]-2-(Fmoc-Amino)Pentanoic Acid
Appearance
White to off-white powder
Purity
≥ 94% (HPLC)
Density
1.25±0.1 g/cm3(Predicted)
Storage
Store at-20 °C
InChI
InChI=1S/C31H40N4O8/c1-30(2,3)42-28(39)34-26(32)35(29(40)43-31(4,5)6)17-11-16-24(25(36)37)33-27(38)41-18-23-21-14-9-7-12-19(21)20-13-8-10-15-22(20)23/h7-10,12-15,23-24H,11,16-18H2,1-6H3,(H,33,38)(H,36,37)(H2,32,34,39)/t24-/m0/s1
InChI Key
QAWFIDADTYJUPT-DEOSSOPVSA-N
Canonical SMILES
CC(C)(C)OC(=O)N=C(N)N(CCCC(C(=O)O)NC(=O)OCC1C2=CC=CC=C2C3=CC=CC=C13)C(=O)OC(C)(C)C

Nα-Fmoc-Nω,Nω'-bis-Boc-L-arginine, a shielded iteration of the amino acid arginine widely utilized in peptide synthesis, boasts a multitude of applications. Here are the key applications intricately presented with high perplexity and burstiness:

Peptide Synthesis: Central to the art of peptide synthesis, Nα-Fmoc-Nω,Nω'-bis-Boc-L-arginine assumes a crucial role in the meticulous orchestration of solid-phase peptide assembly. The strategic integration of Fmoc and Boc shielding safeguards the reactive amino and guanidino groups of arginine, effectively thwarting undesired side reactions that may arise during the synthesis journey. Upon the culmination of the synthetic endeavor, these protective entities are meticulously removed, unveiling the liberated peptide for subsequent in-depth biological inquiries.

Pharmaceutical Development: Positioned at the forefront of pharmaceutical innovation, Nα-Fmoc-Nω,Nω'-bis-Boc-L-arginine emerges as a cornerstone ingredient in the intricate formulation and construction of peptide-centric medicinal compounds. Within its shielded state lies the facilitation of precise chemical manipulations, enabling the construction of elaborate peptide architectures with unparalleled accuracy. This precision plays a pivotal role in nurturing the development of therapeutic peptides endowed with heightened stability, specificity, and efficacy - underscoring its indispensable role in the realm of drug innovation.

Bioconjugation Techniques: The fusion of peptides with a diverse array of entities, spanning from pharmaceuticals to fluorescent tags or polymers, frequently demands the utilization of shielded amino acids such as Nα-Fmoc-Nω,Nω'-bis-Boc-L-arginine. This utilization allows for the creation of well-defined bioconjugates tailored for targeted drug dissemination, imaging procedures, and diagnostic ventures. The protective groups delicately preserve the structural integrity of the arginine residue throughout the bioconjugation process, ensuring the retention of its functional properties for the effective synthesis of bioconjugates tailored to specific applications.

Structural Biology: Within the intricate domain of structural biology, researchers harness the potential of Nα-Fmoc-Nω,Nω'-bis-Boc-L-arginine to delve into the complexities of protein structure and function with unparalleled depth. By incorporating this shielded amino acid into synthetic peptides, scientists can meticulously examine the contributions of arginine residues to pivotal aspects such as protein folding, stability, and intermolecular interactions. This profound insight serves as a cornerstone for unraveling the dynamic mechanisms governing protein behavior, ultimately guiding the design of innovative protein-derived therapeutic interventions and propelling the field of structural biology towards unprecedented horizons.

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.
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