Name: Boc-Phe-(Alloc)Lys-PAB-PNP
Brand: BOC Sciences
Rating: 5 (1 reviews)

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Synonyms

[4-[[(2S)-1-amino-1-oxo-6-(prop-2-enoxycarbonylamino)hexan-2-yl]-[(2S)-2-[(2-methylpropan-2-yl)oxycarbonylamino]-3-phenylpropanoyl]amino]phenyl]methyl (4-nitrophenyl) carbonate;

IUPAC Name

[4-[[(2S)-1-amino-1-oxo-6-(prop-2-enoxycarbonylamino)hexan-2-yl]-[(2S)-2-[(2-methylpropan-2-yl)oxycarbonylamino]-3-phenylpropanoyl]amino]phenyl]methyl (4-nitrophenyl) carbonate

Canonical SMILES

CC(C)(C)OC(=O)NC(CC1=CC=CC=C1)C(=O)N(C2=CC=C(C=C2)COC(=O)OC3=CC=C(C=C3)[N+](=O)[O-])C(CCCCNC(=O)OCC=C)C(=O)N

InChI

InChI=1S/C38H45N5O11/c1-5-23-51-35(46)40-22-10-9-13-32(33(39)44)42(34(45)31(24-26-11-7-6-8-12-26)41-36(47)54-38(2,3)4)28-16-14-27(15-17-28)25-52-37(48)53-30-20-18-29(19-21-30)43(49)50/h5-8,11-12,14-21,31-32H,1,9-10,13,22-25H2,2-4H3,(H2,39,44)(H,40,46)(H,41,47)/t31-,32-/m0/s1

InChIKey

ZFWAEVQMHYNGJL-ACHIHNKUSA-N

Appearance

Soild powder

Shipping

Room temperature, or blue ice upon request.

Boc-Phe-(Alloc)Lys-PAB-PNP, a versatile chemical reagent, finds wide application in peptide synthesis and biochemical research.

Solid-Phase Peptide Synthesis: Playing a pivotal role in solid-phase peptide syntheses, Boc-Phe-(Alloc)Lys-PAB-PNP simplifies the assembly of intricate peptide chains. This reagent facilitates precise and effective coupling reactions during the synthesis process, enabling researchers to craft peptides with meticulously defined sequences for diverse biological experiments.

Drug Development: In the arena of pharmaceutical research, this reagent serves as a cornerstone in the creation of peptide-based drug candidates. By incorporating Boc-Phe-(Alloc)Lys-PAB-PNP, scientists can engineer peptides with promising therapeutic attributes. These artificially synthesized peptides undergo rigorous testing to evaluate their efficacy and safety as potential drug candidates, driving innovation in the field of medicine.

Proteomics: Embraced by the discipline of proteomics, Boc-Phe-(Alloc)Lys-PAB-PNP aids in the production of crucial peptide standards. These standards play a pivotal role in mass spectrometry-based proteomic analyses, facilitating the identification and quantification of proteins in complex biological samples. The meticulous synthesis of peptides using this reagent ensures the precision and reliability of proteomic investigations.

Chemical Biology: Within the realm of chemical biology, this reagent emerges as a valuable asset for crafting peptide probes and inhibitors. Researchers leverage Boc-Phe-(Alloc)Lys-PAB-PNP to synthesize peptides capable of selectively binding to or impeding specific proteins. These tailored peptide probes serve as indispensable instruments for investigating protein functionality and interactions within intricate biological systems, unveiling novel insights into the molecular world.

1. Synthesis of different types of dipeptide building units containing N- or C-terminal arginine for the assembly of backbone cyclic peptides

L Seyfarth, S Reissmann, C Schumann, G Greiner J Pept Res . 2000 Jun;55(6):428-35. doi: 10.1034/j.1399-3011.2000.00719.x.

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. HYCRAM technology was applied using the Boc-Arg(Alloc)2-OH derivative and the Fmoc group to protect the aminoalkyl function. The reduced peptide bond was prepared by reductive alkylation of the arginine derivative with the Boc-protected amino aldehyde, derived from Boc-Phe-OH. The best results for condensation of the branching chain to the reduced peptide bond were obtained using mixed anhydrides. Both types of dipeptide building units can be used in solid-phase synthesis in the same manner as amino acid derivatives.