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H-D-Asn(Trt)-2-chlorotrityl resin

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

2-Chlorotrityl-Chloride-Resin is less acid-labile than Trityl Resin, and is widely used for solid phase immobilization. It has been used with the Fmoc/tBu methodology in the microwave-assisted solid phase peptide synthesis.

Category

2-Chlorotrityl-Chloride-Resin with Amino Acids

Catalog number

BAT-000561

Synonyms

H-D-Asn(Trt)-Trt(2-Cl)-Resin; H-D-Asn(Trt)-Barlos Resin; N-γ-Trityl-D-asparagine 2-chlorotrityl resin

DVB Crosslinking

1% DVB

Substitution

1.0-1.4 meq/g

Storage

Store at 2-8 °C

H-D-Asn(Trt)-2-chlorotrityl resin is a solid-phase synthesis resin commonly used in peptide synthesis. Here are some key applications of H-D-Asn(Trt)-2-chlorotrityl resin:

Peptide Synthesis: H-D-Asn(Trt)-2-chlorotrityl resin is essential in the solid-phase synthesis of peptides, allowing for the sequential addition of amino acids. It provides a stable link between the growing peptide chain and the solid support, facilitating easy purification. The Trt (trityl) group protecting the asparagine ensures that side reactions are minimized during synthesis.

Combinatorial Chemistry: In combinatorial chemistry, H-D-Asn(Trt)-2-chlorotrityl resin is used to create vast libraries of peptides for drug discovery and development. By enabling the efficient synthesis of diverse peptide sequences, this resin helps in identifying potential lead compounds. Screening these libraries accelerates the discovery process and aids in finding new therapeutic candidates.

Bioconjugation: The H-D-Asn(Trt)-2-chlorotrityl resin can be used for the synthesis of bioconjugates, such as peptide-drug conjugates, which are crucial in targeted therapies. By facilitating the attachment of biologically active peptides to other molecules, this resin plays a role in the development of precision medicine. The stability and ease of cleavage from the resin ensure high-yield and high-purity products.

Structural Biology: In structural biology, high-purity peptides synthesized using H-D-Asn(Trt)-2-chlorotrityl resin are used for crystallography and NMR studies. These peptides help in elucidating protein structures, protein-ligand interactions, and conformational studies. The ability to produce specific peptide sequences assists researchers in understanding molecular mechanisms and protein dynamics.

1. Convergent Synthesis of Thioether Containing Peptides

Spyridon Mourtas, Christina Katakalou, Dimitrios Gatos, Kleomenis Barlos Molecules. 2020 Jan 5;25(1):218. doi: 10.3390/molecules25010218.

Thioether containing peptides were obtained following three synthetic routes. In route A, halo acids esterified on 2-chlorotrityl(Cltr) resin were reacted with N-fluorenylmethoxycarbonyl (Fmoc) aminothiols. These were either cleaved from the resin to the corresponding (Fmoc-aminothiol)carboxylic acids, which were used as key building blocks in solid phase peptide synthesis (SPPS), or the N-Fmoc group was deprotected and peptide chains were elongated by standard SPPS. The obtained N-Fmoc protected thioether containing peptides were then condensed either in solution, or on solid support, with the appropriate amino components of peptides. In route B, the thioether containing peptides were obtained by the reaction of N-Fmoc aminothiols with bromoacetylated peptides, which were synthesized on Cltr-resin, followed by removal of the N-Fmoc group and subsequent peptide elongation by standard SPPS. In route C, the thioether containing peptides were obtained by the condensation of a haloacylated peptide synthesized on Cltr-resin and a thiol-peptide synthesized either on 4-methoxytrityl(Mmt) or trityl(Trt) resin.

2. 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.

3. Solid-Phase Insertion of N-mercaptoalkylglycine Residues into Peptides

Spyridon Mourtas, Dimitrios Gatos, Kleomenis Barlos Molecules. 2019 Nov 22;24(23):4261. doi: 10.3390/molecules24234261.

N-mercaptoalkylglycine residues were inserted into peptides by reacting N-free amino groups of peptides, which were initially synthesized on 2-chlorotrityl resin (Cltr) using the Fmoc/tBu method, with bromoacetic acid and subsequent nucleophilic replacement of the bromide by reacting with S-4-methoxytrityl- (Mmt)/S-trityl- (Trt) protected aminothiols. The synthesized thiols containing peptide-peptoid hybrids were cleaved from the resin, either protected by treatment with dichloromethane (DCM)/trifluoroethanol (TFE)/acetic acid (AcOH) (7:2:1), or deprotected (fully or partially) by treatment with trifluoroacetic acid (TFA) solution using triethylsilane (TES) as a scavenger.