Nα-Fmoc-D-glutamine 4-alkoxybenzyl alcohol resin
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Nα-Fmoc-D-glutamine 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-000199
Synonyms
Fmoc-D-Gln-Wang resin
DVB Crosslinking
1% DVB
Mesh Size
100-200 mesh
Substitution
0.1-0.5 mmol/g
Storage
Store at 2-8°C

Nα-Fmoc-D-glutamine 4-alkoxybenzyl alcohol resin is a specialized resin used in solid-phase peptide synthesis, serving as an essential tool in peptide and protein chemistry. Here are some key applications of this resin:

Peptide Synthesis: This resin is widely employed in the synthesis of peptides, allowing for the precise addition of amino acids in a sequence-specific manner. The Fmoc protection strategy provides selectivity and control during the synthesis process. It is central to producing peptides for research in drug development, structural biology, and enzymology.

Combinatorial Chemistry: Nα-Fmoc-D-glutamine 4-alkoxybenzyl alcohol resin facilitates the generation of peptide libraries through combinatorial chemistry. These libraries enable the screening and identification of bioactive peptides with potential therapeutic applications. This approach is invaluable in drug discovery and the development of new peptide-based drugs.

Structural Biology: Through peptide synthesis, this resin aids in the creation of small protein fragments or mimetics for structural studies. By synthesizing specific segments of proteins, researchers can investigate their structure-function relationships using techniques such as NMR or X-ray crystallography. This plays a critical role in understanding protein dynamics and interactions.

Bioconjugation: The resin is also used in bioconjugation applications where synthesized peptides are linked to various biomolecules or surfaces. This application is crucial in the development of peptide-based vaccines, diagnostic tools, and therapeutic delivery systems. The versatile chemistry of the resin supports the creation of highly specific and functionalized conjugates.

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.
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