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Application Area

Fmoc-Asn-OPfp

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

Category

Fluorinated Amino Acids

Catalog number

BAT-005296

CAS number

86060-99-3

Molecular Formula

C25H17N2O5F5

Molecular Weight

520.41

IUPAC Name

(2,3,4,5,6-pentafluorophenyl) (2S)-4-amino-2-(9H-fluoren-9-ylmethoxycarbonylamino)-4-oxobutanoate

Synonyms

(2,3,4,5,6-pentafluorophenyl)(2S)-4-amino-2-(9H-fluoren-9-ylmethoxycarbonylamino)-4-oxobutanoate; Fmoc-L-asparagine pentafluorophenyl ester; Fmoc-Asn-pentafluorophenyl ester

Appearance

White powder

Purity

≧ 95%

Density

1.478±0.060 g/cm3

Melting Point

160 °C

Boiling Point

702.4±60.0 °C

Storage

Store at 2-8 °C

InChI

InChI=1S/C25H17F5N2O5/c26-18-19(27)21(29)23(22(30)20(18)28)37-24(34)16(9-17(31)33)32-25(35)36-10-15-13-7-3-1-5-11(13)12-6-2-4-8-14(12)15/h1-8,15-16H,9-10H2,(H2,31,33)(H,32,35)/t16-/m0/s1

InChI Key

FESVUEALWMQZEP-INIZCTEOSA-N

Canonical SMILES

C1=CC=C2C(=C1)C(C3=CC=CC=C32)COC(=O)NC(CC(=O)N)C(=O)OC4=C(C(=C(C(=C4F)F)F)F)F

Fmoc-Asn-OPfp, a protected amino acid derivative crucial for peptide synthesis, finds diverse applications in research and industry. Here are four key uses of Fmoc-Asn-OPfp elaborated with high perplexity and burstiness:

Solid-Phase Peptide Synthesis: Serving as a cornerstone in solid-phase peptide synthesis, Fmoc-Asn-OPfp plays a pivotal role in appending asparagine residues to the nascent peptide chain. The Fmoc protecting group aids in precise peptide bond formation, while the pentafluorophenyl ester (OPfp) boosts coupling efficiency. This meticulous process ensures the synthesis of pure peptides essential for advanced research endeavors and therapeutic interventions.

Protein Engineering: Delving into the realm of protein engineering, Fmoc-Asn-OPfp emerges as a key player in crafting proteins with distinct asparagine-rich motifs. By integrating Fmoc-Asn-OPfp into peptide synthesis protocols, researchers embark on a journey to unravel the structural and functional significance of asparagine residues within proteins. This approach stands as a fundamental pillar in deciphering protein folding dynamics, stability, and intricate molecular interactions.

Drug Development: Stepping into the realm of pharmaceutical innovation, Fmoc-Asn-OPfp takes center stage in sculpting peptide-based drug candidates. Peptides containing asparagine exhibit potent bioactive properties, such as enzyme inhibition or receptor binding. By harnessing Fmoc-Asn-OPfp in the synthesis process, researchers unlock the potential to create novel peptides with therapeutic implications.

Bioconjugation Studies: In the realm of bioconjugation, Fmoc-Asn-OPfp emerges as a versatile tool for linking peptides to an array of molecules like fluorescent dyes, enzymes, or antibodies. The asparagine residue serves as a linchpin or functional node in these conjugates, enabling in-depth exploration of biological interactions. This strategic use facilitates the development of cutting-edge diagnostic tools and targeted delivery systems, propelling forward the frontiers of bioconjugation science.

1. Multiple synthesis by the multipin method as a methodological tool

A M Bray, R M Valerio, A J DiPasquale, J Greig, N J Maeji J Pept Sci. 1995 Jan-Feb;1(1):80-7. doi: 10.1002/psc.310010110.

The multipin method of peptide synthesis is demonstrated as a potent methodological tool, where large numbers of comparative studies can be performed concurrently. Two studies are presented. In each study, the test peptides were simultaneously synthesized, and the products examined by high throughput ion spray mass spectrometry and reverse-phase HPLC. In the first study, comprising 24 experiments, peptides 1 (AELFSTHYLAFKEDYSQ-NH2) and 2 (LKDFRVYFREGRDQLWKGPG-NH2) were prepared using Fmoc-Axx/BOP/HOBt/NMM [100 : 100 : 100 : 150 mM) and Fmoc-AXX/HATU/HOAt/NMM (100 : 100 : 100 : 150 nM) with 60, 90 and 120 min coupling times. The two reagent combinations were found to give comparable results. The second study compared the N-terminal coupling of Fmoc-Asn-OH, Fmoc-Asn(Mbh)-OH, Fmoc-Asn(Mtt)-OH, Fmoc-Asn(Tmob)-OH and Fmoc-Asn(Trt)-OH in the synthesis of seven test peptides: 3, NVQAAIDYIG-cyclo(KP): 4. NTVQAAIDYIG-cyclo(KP): 5. NRVYVHPFNL: 6. NRVYVHPFHL: 7. NEAYVHDAPVRSLN: 8. NQLVVPSEGLYLIYSQVLFK; 9, NPNANPNANPNA. A total of 33 experiments were performed. Peptides 3 and 4 were selected to highlight the effect of steric bulk of each Asn derivative on coupling efficiency. Reagent efficiency, as measured by target peptide purity, was as follows: Fmoc-Asn(Tmob)-OH > Fmoc-Asn-OH > Fmoc-Asn(Mtt)-OH = Fmoc-Asn(Trt)-OH > Fmoc-Asn(Mbh)-OH.

2. Novel N omega-xanthenyl-protecting groups for asparagine and glutamine, and applications to N alpha-9-fluorenylmethyloxycarbonyl (Fmoc) solid-phase peptide synthesis

Y Han, N A Solé, J Tejbrant, G Barany Pept Res. 1996 Jul-Aug;9(4):166-73.

The N alpha-9-fluorenylmethyloxycarbonyl (Fmoc), N omega-9H-xanthen-9-yl (Xan), N omega-2-methoxy-9H-xanthen-9-yl (2-Moxan) or N omega-3-methoxy-9H-xanthen-9-yl (3-Moxan) derivatives of asparagine and glutamine were prepared conveniently by acid-catalyzed reactions of appropriate xanthydrols with Fmoc-Asn-OH and Fmoc-Gln-OH. The Xan and 2-Moxan protected derivatives have been used in Fmoc solid-phase syntheses of several challenging peptides: a modified Riniker's peptide to probe tryptophanalkylation side reactions, Briand's peptide to assess deblocking, at the N-terminus and Marshall's ACP (65-74) to test difficult couplings. Removal of the Asn and Gln side-chain protection occurred concomitantly with release of peptide from the support, under the conditions for acidolytic cleavage of the tris(alkoxy)benzylamide (PAL) anchoring linkage by use of trifluoroacetic acid/scavenger mixtures. For each of the model peptides, the products obtained by the new protection schemes were purer than those obtained with N omega-2,4,6-trimethoxybenzyl (Tmob) or N omega-triphenylmethyl (Trt) protection for Asn and Gln.

3. Efficient Fmoc/solid-phase synthesis of Abu(P)-containing peptides using Fmoc-Abu(PO3Me2)-OH

J W Perich Int J Pept Protein Res. 1994 Sep;44(3):288-94. doi: 10.1111/j.1399-3011.1994.tb00172.x.

The synthesis of the two 4-phosphono-2-aminobutanoyl-containing peptides, Leu-Arg-Arg-Val-Abu(P)-Leu-Gly-OH.CF3CO2H and Ile-Val-Pro-Asn-Abu(P)-Val-Glu-Glu-OH.CF3CO2H was accomplished by the use of Fmoc-Abu(PO3Me2)-OH in Fmoc/solid-phase peptide synthesis. The protected phosphoamino acid, Fmoc-Abu(PO3Me2)-OH, was prepared from Boc-Asp-OtBu in seven steps, the formation of the C-P linkage being effected by the treatment of Boc-Asa-OtBu with dimethyl trimethylsilyl phosphite. Peptide synthesis was performed using Wang Resin as the polymer support with both peptides assembled by the use of PyBOP for the coupling of Fmoc amino acids and 20% piperidine for cleavage of the Fmoc group from the Fmoc-peptide after each coupling cycle. Cleavage of the peptide from the resin and peptide deprotection was accomplished by the treatment of the peptide-resin with 5% thioanisole/TFA followed by cleavage of the methyl phosphonate group by 1 M bromotrimethylsilane/1 M thioanisole in TFA.