1234692-66-0

Usage

Uses

Used in Peptide Synthesis:
2S-[[(9H-fluoren-9-ylmethoxy)carbonyl]amino]-5-hexynoic acid is used as a building block for the synthesis of peptide and protein molecules. Its unique structure allows for the incorporation of the hexynoic acid group into the peptide chain, which can be useful for various applications, such as the development of new drugs or the study of protein structure and function.
Used in Solid-Phase Peptide Synthesis:
In the field of solid-phase peptide synthesis, 2S-[[(9H-fluoren-9-ylmethoxy)carbonyl]amino]-5-hexynoic acid is used as a key component in the synthesis process. The fluorenylmethyloxycarbonyl group enables selective removal and protection of the amino group, facilitating the stepwise assembly of peptide chains on an insoluble resin support.
Used in Biochemistry and Molecular Biology Research:
2S-[[(9H-fluoren-9-ylmethoxy)carbonyl]amino]-5-hexynoic acid is also used in biochemistry and molecular biology research. Its unique structure and the presence of the fluorenylmethyloxycarbonyl group make it a useful tool for studying protein interactions, modifications, and functions, as well as for the development of new techniques and methods in these fields.

Upstream product

• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 102774-86-7 9-fluorenylmethyl N-succinimidyl carbonate 
• 98891-36-2 (S)-2-amino-5-hexynoic acid 
• 38771-21-0 4-bromobut-1-yne 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 

Relevant academic research and scientific papers

Design of triazole-stapled BCL9 α-helical peptides to target the β-catenin/B-cell CLL/lymphoma 9 (BCL9) protein-protein interaction

The interaction between β-catenin and B-cell CLL/lymphoma 9 (BCL9), critical for the transcriptional activity of β-catenin, is mediated by a helical segment from BCL9 and a large binding groove in β-catenin. Design of potent, metabolically stable BCL9 peptides represents an attractive approach to inhibit the activity of β-catenin. In this study, we report the use of the Huisgen 1,3-dipolar cycloaddition reaction to generate triazole-stapled BCL9 α-helical peptides. The high efficiency and mild conditions of this "click" reaction combined with the ease of synthesis of the necessary unnatural amino acids allows for facile synthesis of triazole-stapled peptides. We have performed extensive optimization of this approach and identified the optimal combinations of azido and alkynyl linkers necessary for stapling BCL9 helices. The unsymmetrical nature of the triazole staple also allowed the synthesis of double-stapled BCL9 peptides, which show a marked increase in helical character and an improvement in binding affinity and metabolic stability relative to wild-type and linear BCL9 peptides. This study lays the foundation for further optimization of these triazole-stapled BCL9 peptides as potent, metabolically stable, and cell-permeable inhibitors to target the β-catenin and BCL9 interaction.

An Optimized Synthesis of Fmoc- l -Homopropargylglycine-OH

An efficient multigram synthesis of alkynyl amino acid Fmoc-l-homopropargylglycine-OH is described. A double Boc protection is optimized for high material throughput, and the key Seyferth-Gilbert homologation is optimized to avoid racemization. Eighteen grams of the enantiopure (>98% ee) noncanonical amino acid was readily generated for use in solid phase synthesis to make peptides that can be functionalized by copper-assisted alkyne-azide cycloaddition.

Improved synthesis of unnatural amino acids for peptide stapling

The procedures for the synthesis of various α-alkenyl and alkyne amino acids were systematically optimized in light of enhancing atom economy, reducing hazardous reagent usage, and simplifying workup. By starting with Boc-Pro-OH and coupling with EDCI/DMAP followed by alkylation, chiral auxiliary was synthesized with high yield and enantioselectivity. For alkylation of the chiral complex, tBuONa was found and proved by quantitative calculation to be superior to tBuOK in generating more nucleophilic enolate salt, thereby can significantly enhance yield under room temperature. Final Fmoc protection was also dramatically facilitated in one-pot sequential manner by adding EDTA-2Na as the nickel chelator. Synthesis of α-bisalkenyl amino acid was also accomplished by achiral complex approach with high yield and efficacy. Accordingly, five most commonly used N-Fmoc protected α-alkenyl and alkynyl amino acids were synthesized and characterized.