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Nα-Fmoc-Nγ-trityl-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-000207

Synonyms

Fmoc-L-Asn(Trt)-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-Nγ-trityl-L-asparagine 4-alkoxybenzyl alcohol resin stands as a specialized tool within solid-phase peptide synthesis (SPPS), offering unparalleled precision and efficiency. Here are the key applications of this resin:

Peptide Synthesis: Central to the synthesis of asparagine-containing peptides, this resin features Fmoc protection on the N-terminal and trityl protection on the side chain amino group, ensuring meticulous deprotection and coupling reactions. This meticulous approach leads to the creation of high-yield, high-fidelity peptide sequences, essential for advancing biochemical and pharmaceutical research endeavors.

Combinatorial Chemistry: Within the realm of combinatorial chemistry, this resin acts as a foundational component for constructing expansive libraries of peptide sequences. Researchers can systematically explore a vast array of peptide structures, uncovering potential bioactive compounds. This acceleration of drug discovery processes provides an extensive repertoire of candidates for therapeutic development, propelling advancements in medicinal science.

Protein-Protein Interaction Studies: Peptides synthesized on this resin serve as valuable tools for investigating protein-protein interactions. Through the generation of specific peptide sequences, researchers delve into binding affinities and interaction dynamics with target proteins. This acquired knowledge plays a pivotal role in unraveling complex biochemical pathways and designing inhibitors or activators to modulate protein functions, shaping the landscape of biotechnological research.

Vaccine Development: Leveraging the capabilities of this resin in peptide synthesis, scientists drive forward advancements in vaccine development. The precise arrangement of amino acid sequences plays a crucial role in eliciting immune responses necessary for vaccine efficacy. By crafting peptides that mirror pathogen epitopes, researchers design vaccines capable of stimulating protective immunity, offering promising solutions in combating infectious diseases and cancer.

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.