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

Name: Nα-Fmoc-L-glutamine 4-alkoxybenzyl alcohol resin
Brand: BOC Sciences
Rating: 5 (1 reviews)

* 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-000180

Synonyms

Fmoc-L-Gln-Wang resin

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-glutamine 4-alkoxybenzyl alcohol resin plays a pivotal role in solid-phase peptide synthesis, serving as a specialized reagent with diverse applications.

Peptide Synthesis: Utilized as a solid support for peptide synthesis, this resin aids in the orchestrated assembly of amino acids into precise sequences. Its employment ensures the synthesis of peptides with exceptional fidelity and purity, imperative for applications in therapeutics, research, and biochemical investigations. This methodical approach is fundamental for developing peptides tailored for specific purposes, underpinning advancements in various fields.

Bioconjugation: The utility of Nα-Fmoc-L-glutamine 4-alkoxybenzyl alcohol resin extends to bioconjugation, facilitating the attachment of diverse functional groups to create peptide conjugates. This process is instrumental in crafting peptide-based probes and drugs, enabling researchers to introduce modifications that enhance peptide stability, solubility, and biological efficacy. Such capabilities open avenues for innovative drug design and targeted therapeutics, enriching the toolkit for biochemists and pharmacologists.

Chemical Biology: In the realm of chemical biology, this specialized resin empowers researchers to delve deep into protein-peptide interactions by synthesizing peptides with specific sequences and alterations. This approach forms the bedrock of molecular level investigations, shedding light on intricate biological processes. By manipulating peptide structures, scientists can explore the nuances of protein function and dynamics within living cells.

Proteomics: Within the domain of proteomics, this resin facilitates the synthesis of isotope-labeled peptides crucial for quantitative proteomic analyses. Such applications are indispensable for identifying and quantifying proteins within complex mixtures, providing insights into proteome dynamics and offering a gateway to unraveling disease biomarkers. This capability fuels advancements in biomolecular research, enabling a deeper understanding of protein behavior and signaling pathways critical for disease diagnosis and treatment strategies.

1. 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.

2. 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.

3. 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.