Fmoc-Glu(OtBu)-Alko-PEG Resin
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Fmoc-Glu(OtBu)-Alko-PEG Resin

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

Wang resins are the standard supports for the preparation of peptide acids by the Fmoc batch solid phase synthesis strategy. Fmoc amino acids are pre-loaded to Wang resins so that that epimerization and dipeptide formation are minimized.

Category
Wang Resin with Amino Acids
Catalog number
BAT-001128
Synonyms
Fmoc-Glu(OtBu)-Wang-PEG Resin; N-α-(9-Fluorenylmethoxycarbonyl)-L-glutamic acid γ-t-butyl ester p-methoxybenzyl alcohol polyethyleneglycol resin
DVB Crosslinking
1% DVB
Substitution
1.0-1.4 meq/g
Storage
Store at 2-8 °C

Fmoc-Glu(OtBu)-Alko-PEG Resin, a specialized resin crucial in solid-phase peptide synthesis (SPPS), plays a pivotal role in attaching specific peptide sequences with meticulous precision. Here are four key applications of Fmoc-Glu(OtBu)-Alko-PEG Resin:

Peptide Synthesis: Utilizing this resin in SPPS results in the synthesis of peptides with exceptional accuracy and efficiency. The Fmoc group transiently shields the amino group, facilitating the sequential addition of amino acids. This widely employed method is instrumental in generating peptides for diverse purposes, spanning from research endeavors to therapeutic advancements and biomaterial innovations.

Drug Delivery Systems: Fmoc-Glu(OtBu)-Alko-PEG Resin plays a crucial role in developing peptide-based drug delivery systems. By affixing peptides to the resin, researchers engineer systems that precisely target specific cells or tissues, thereby enhancing drug delivery efficacy and specificity.

Functional Bioconjugates: Employing the resin, researchers create bioconjugates by connecting peptides to various biomolecules like proteins, antibodies, or polymers. These bioconjugates are essential components in diagnostic assays, therapeutic agents, and targeted imaging techniques. The resin’s versatility enables the formation of intricate and diverse bioconjugate structures.

Material Science: In the realm of materials science, Fmoc-Glu(OtBu)-Alko-PEG Resin serves as a cornerstone in fabricating peptide-based hydrogels and biomaterials. The resin facilitates the integration of peptide sequences that can autonomously assemble, enriching material attributes such as biocompatibility and mechanical robustness. These tailor-made materials find applications in vital areas like tissue engineering, wound healing, and regenerative medicine, representing a realm of innovation at the intersection of biology and material science.

1. 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.
2. Solid-phase synthesis of peptides with C-terminal asparagine or glutamine. An effective, mild procedure based on N alpha-fluorenylmethyloxycarbonyl (Fmoc) protection and side-chain anchoring to a tris(alkoxy)benzylamide (PAL) handle
F Albericio, R van Abel, G Barany Int J Pept Protein Res. 1990 Mar;35(3):284-6.
Attempts to anchor Fmoc-asparagine or glutamine as p-alkoxybenzyl esters for solid-phase peptide synthesis are fraught with difficulties. A convenient and effective method to prepare peptides with C-terminal asparagine or glutamine involves quantitative attachment of N alpha-Fmoc-C alpha-tert.-butyl aspartate or glutamate via the free omega-carboxyl groups to a tris(alkoxy)benzylamino (PAL) support. Chain elongation proceeds normally by standard Fmoc chemistry, and treatment with acid, e.g., CF3COOH--CH2Cl2, 90 min at 25 degrees, releases the desired peptides in greater than 95% yields without side reactions at the C-terminus. Feasibility of the approach has been demonstrated by the syntheses of the C-terminal octapeptide from human proinsulin, H-Leu-Ala-Leu-Glu-Gly-Ser-Leu-Gln-OH, and the serum thymic factor pGlu-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn-OH.
3. Asparagine coupling in Fmoc solid phase peptide synthesis
H Gausepohl, M Kraft, R W Frank Int J Pept Protein Res. 1989 Oct;34(4):287-94. doi: 10.1111/j.1399-3011.1989.tb01576.x.
To investigate side reactions during the activation of side chain unprotected asparagine in Fmoc-solid phase peptide synthesis the peptide Met-Lys-Asn-Val-Pro-Glu-Pro-Ser was synthesized using different coupling conditions for introduction of the asparagine residue. Asparagine was activated by DCC/HOBt, BOP (Castro's reagent) or introduced as the pentafluorophenyl ester. The resulting peptide products were analyzed by HPLC, mass spectrometry and Edman degradation. In the crude products varying amounts of beta-cyano alanine were found, which had been formed by dehydration of the side chain amide during carboxyl activation of Fmoc-asparagine. A homogeneous peptide was obtained by using either side chain protected asparagine derivatives with BOP mediated activation or by coupling of Fmoc-Asn-OPfp. Fmoc-Asn(Mbh)-OH and Fmoc-Asn(Tmob)-OH were coupled rapidly and without side reactions with BOP. For the side chain protected derivatives the coupling was as fast as that of other Fmoc-amino acid derivatives, whereas couplings of Fmoc-Asn-OH proceed more slowly. However, during acidolytic cleavage both protection groups, Mbh and Tmob, generate carbonium ions which readily alkylate tryptophan residues in a peptide. Tryptophan modification was examined using the model peptide Asn-Trp-Asn-Val-Pro-Glu-Pro-Ser. Alkylation could be reduced by addition of scavengers to the TFA during cleavage and side chain deprotection. A homogeneous peptide containing both, asparagine and tryptophan, was obtained only by coupling of Fmoc-Asn-OPfp.
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