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Nα-Fmoc-L-asparagine 4-alkoxybenzyl alcohol resin

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

Pre-loaded resins for solid phase peptide and organic synthesis

Category

Wang Resin with Amino Acids

Catalog number

BAT-000200

Synonyms

Fmoc-L-Asn-Wang resin

Appearance

Pale yellow beads

DVB Crosslinking

1% DVB

Mesh Size

100-200 mesh

Substitution

0.3-0.8 meq/g

Storage

Store at 2-8°C

Nα-Fmoc-L-asparagine 4-alkoxybenzyl alcohol resin is a specialized chemical reagent utilized in peptide synthesis and various biochemical applications. Here are the key applications of this resin presented with high perplexity and burstiness:

Peptide Synthesis: Playing a pivotal role in solid-phase peptide synthesis (SPPS), Nα-Fmoc-L-asparagine 4-alkoxybenzyl alcohol resin enables the meticulous stepwise construction of peptides. Its unique structure facilitates efficient coupling and deprotection processes crucial for synthesizing intricate peptides. This indispensable reagent ensures exceptional purity and yield, serving as a cornerstone in peptide research and the development of novel drugs.

Protein Engineering: Within the realm of protein engineering, this resin is harnessed to craft peptide sequences featuring essential asparagine residues pivotal for protein functionality and interaction analyses. By synthesizing peptides with precise asparagine incorporations, researchers can delve into protein folding, stability, and activity dynamics. This versatile tool aids in engineering novel proteins endowed with desirable attributes for both therapeutic and industrial applications.

Antibody Production: Leveraging Nα-Fmoc-L-asparagine 4-alkoxybenzyl alcohol resin in generating asparagine-rich peptides is key to producing antigenic peptides essential for antibody elicitation. These peptides act as epitopes, eliciting targeted immune responses and fostering the generation of high-affinity antibodies. This critical application lies at the forefront of diagnostic tool development and the advancement of cutting-edge therapeutic antibody treatments.

Drug Discovery: Integral to the synthesis of peptide-based drug candidates, this resin is pivotal in targeting specific asparagine residues within disease-associated proteins. In the realm of drug discovery, the precision in asparagine incorporation empowers the design of peptides adept at binding effectively to their designated targets.

1. Quantitative assessment of preloaded 4-alkoxybenzyl alcohol resins for solid-phase peptide syntheses by 1D and 2D HR-MAS NMR

Daniel Rentsch, Christian Stähelin, Markus Obkircher, Roland Hany, Marina Simeunovic, Daniel Samson, Günther Loidl, Fritz Dick ACS Comb Sci. 2012 Nov 12;14(11):613-20. doi: 10.1021/co3000924. Epub 2012 Oct 23.

The quality of preloaded Wang resins is very important for the success of solid-phase peptide syntheses (SPPS). A critical factor is the capping of remaining hydroxyl groups after loading with the first amino acid, since these free alcohols lead to truncated sequences during the following SPPS steps. Because the detection of hydroxyl groups by color tests is difficult and unreliable, the capping efficiency is often controlled by time-consuming peptide test syntheses. Here, we describe a two-dimensional, high resolution magic angle spinning NMR method for the quantitative determination of remaining 4-alkoxybenzyl alcohols in Fmoc-Xaa-Wang resins with a detection limit of 1 mol-%. The NMR method was validated with samples of known ratios between Fmoc-Ala-Wang and 4-alkoxybenzylalcohol resin. Application to a set of preloaded Fmoc-Ala- and Fmoc-Thr(tBu)-Wang test resins demonstrated that the full range of essential amino acids can be quantified without further spectrometer calibration. Compared to established test synthesis protocols, the NMR method represents not only advantages in terms of time and cost savings but also eliminates all inaccuracies due to further sample treatment like SPPS and cleavage from the resin.

2. 4-Chloromethylphenoxyacetyl polystyrene and polyamide supports for solid-phase peptide synthesis

R Colombo, E Atherton, R C Sheppard, V Woolley Int J Pept Protein Res. 1983 Feb;21(2):118-26. doi: 10.1111/j.1399-3011.1983.tb03085.x.

Two functionalised supports for the solid-phase synthesis of peptides under mild reaction conditions were prepared: 4-chloromethylphenoxyacetamidomethyl-copoly (styrene-1%-divinylbenzene) and 4-chloromethylphenoxyacetyl-norleucyl-poly (dimethylacrylamide). They were devised in order to avoid the danger of racemization which exists during base-catalyzed esterification of the first protected amino acid to the 4-alkoxybenzyl alcohol resins formerly employed in combination with N alpha-9-fluorenylmethoxycarbonyl and tert.-butyl side-chain protecting groups. Esterification of N alpha-protected amino acids to the new resins can be achieved easily and without significant levels of racemization by means of their caesium salts, while cleavage from the supports is possible by treatment with trifluoroacetic acid. The 4-chloromethylphenoxyacetyl polystyrene resin was tested by the synthesis of Leu-enkephalin which was cleaved, at the end of the synthesis, from the solid support in 91% yield by 60% trifluoroacetic acid in methylene chloride, and was shown to be more than 99% pure by ion-exchange chromatography and reverse phase high pressure liquid chromatography.

3. Esterification of 9-fluorenylmethoxycarbonyl-glycosylated serine and cysteine derivatives with an hydroxymethyl resin

E Harth-Fritschy, D Cantacuzène J Pept Res. 1997 Dec;50(6):415-20. doi: 10.1111/j.1399-3011.1997.tb01204.x.

Esterification of glycosylated serine and cysteine derivatives with a 4-alkoxybenzyl alcohol (Wang) resin is described. The classical methods of ester bond formation (symmetrical anhydride, 2-(1H-benzotriazol-1-yl)-1,1,3,3-tetramethyluronium tetrafluoroborate [TBTU]/4-dimethylaminopyridine [DMAP] with or without 1-hydroxybenzotriazole [HOBT], pentafluorophenyl [Pfp] esters gave high percentages of racemization of the glycosylated serine or cysteine residues. To reduce the D-amino acid content, we found that the best results were obtained with the highly efficient MSNT reagent (2,4,6-mesitylenesulfonyl-3-nitro-1,2,4-triazolide), which gave a high yield of substitution of the resin and the lowest percentage of racemization. A difference in behavior was observed between the two amino acids. The glycosylated cysteine derivative always gave lower racemization than the analogous glycosylated serine.