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Fmoc-L-Glutamic(2-chlorotrityl resin)-NH2

Name: Fmoc-L-Glutamic(2-chlorotrityl resin)-NH2
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

2-Chlorotrityl-Chloride-Resin with Amino Acids

Catalog number

BAT-000070

Appearance

Dark brown beads

DVB Crosslinking

1% DVB

Mesh Size

100-200 mesh

Substitution

0.5-0.7 mmol/g

Storage

Store at 2-8°C

Fmoc-L-Glutamic(2-chlorotrityl resin)-NH2 is a specialized product widely utilized in solid-phase peptide synthesis (SPPS) with diverse applications.

Peptide Synthesis: Serving as a foundational material in solid-phase peptide synthesis, Fmoc-L-Glutamic(2-chlorotrityl resin)-NH2 plays a critical role. The 2-chlorotrityl resin acts as a stable and efficient anchor point for the peptide chain’s growth, facilitating the gradual addition of amino acids. This resin ensures the seamless coupling of peptides and easy detachment from the support post-synthesis, guaranteeing high-quality peptide construction through each step.

Custom Peptide Libraries: In the realms of research and pharmaceutical development, Fmoc-L-Glutamic(2-chlorotrityl resin)-NH2 is an invaluable tool for constructing custom peptide libraries for screening purposes. By methodically altering amino acid sequences, scientists can pinpoint peptides with specific biological activities or binding affinities. This method is integral in drug discovery and biochemical research, enabling the identification of novel therapeutic candidates.

Proteomics Studies: The versatile nature of Fmoc-L-Glutamic(2-chlorotrityl resin)-NH2 extends to its application in synthesizing peptides used as standards or probes in proteomics research. These customizable peptides can be modified to detect and quantify proteins in biological samples, facilitating the exploration of protein expression, post-translational modifications, and protein-protein interactions. This tool is instrumental in advancing our understanding of complex protein networks and regulatory processes.

Biomolecular Research: Playing a pivotal role in elucidating protein structure and function, the resin-bound Fmoc-glutamic acid derivative enables the synthesis of peptide fragments or analogs for investigative studies. Researchers can analyze how specific amino acid substitutions influence protein interactions and stability, shedding light on crucial molecular mechanisms. This knowledge is essential for designing novel therapeutic proteins and unraveling the intricacies of biomolecular interactions in biological systems.

1. Application of 2-chlorotrityl resin in solid phase synthesis of (Leu15)-gastrin I and unsulfated cholecystokinin octapeptide. Selective O-deprotection of tyrosine

K Barlos, D Gatos, S Kapolos, C Poulos, W Schäfer, W Q Yao Int J Pept Protein Res. 1991 Dec;38(6):555-61. doi: 10.1111/j.1399-3011.1991.tb01539.x.

The carboxyl terminal dipeptide amide, Fmoc-Asp-Phe-NH2, of gastrin and cholecystokinin (CCK) has been attached in high yield through its free side chain carboxyl group to the acid labile 2-chlorotrityl resin. The obtained peptide resin ester has been applied in the solid phase synthesis of partially protected (Leu15)-gastrin I utilising Fmoc-amino acids. Quantitative cleavage of this peptide from resin, with the t-butyl type side chain protection intact is achieved using mixtures of acetic acid/trifluoroethanol/dichloromethane. Under the same conditions complete detritylation of the tyrosine phenoxy function occurs simultaneously. Thus, the solid-phase synthesis of peptides selectively deprotected at the side chain of tyrosine is rendered possible by the use of 2-chlorotrityl resin and Fmoc-Tyr(Trt)-OH. The efficiency of this approach has been proved by the subsequent high-yield synthesis of three model peptides and the CCK-octapeptide.

2. Synthesis and biological activity of locust AKH-I and its analogues with modifications at the threonine residues

C Poulos, K Karagiannis, M Lee, G Goldsworthy Int J Pept Protein Res. 1994 Dec;44(6):589-93. doi: 10.1111/j.1399-3011.1994.tb01148.x.

A convenient method of synthesis, using a combination of solid and liquid phase methodology, for locust Adipokinetic Hormone-I (AKH-I) and its analogues with modifications at the threonine residues are reported. The N-terminal nonapeptide acid of AKH-I is synthesized in the solid phase using the 2-chlorotrityl chloride resin and the Fmoc/t-Bu strategy. Quantitative cleavage of the nonapeptide acid from the resin, with the tert-butyl type side-chain protection intact, is achieved with a mixture of acetic acid/trifluoroethanol/dichloromethane. The nonapeptide acid is then coupled in solution to the threonine derivatives, H-Thr-NH2 or H-Thr(Bzl)-NH2, with the DCC/HOBt method. The efficiency of this approach in the synthesis of AKH-I is demonstrated by the high yields and purity of the synthesized peptides. All the synthesized peptides were tested in two ways: first, in a lipid mobilization assay in locusts in vivo; and second, in a novel assay in vitro concerned with the uptake of radiolabelled acetate into locust tissue. Replacement of the hydroxyl hydrogen in Thr5 of locust AKH-I by the bulky and highly lipophilic tert-butyl group reduced the potency markedly, whereas efficacy is unaffected, but when the hydroxyl hydrogen of Thr10 in AKH-I is replaced by a benzyl group, the activity of the resulting analogue is identical to that of the natural peptide. Structure-activity relationships are discussed.