288617-72-1

Usage

Uses

Used in Peptide Synthesis:
(S)-N-Fmoc-2-(3'-butenyl)alanine is used as a building block for the synthesis of peptides, providing unique structural and functional properties to the resulting peptides. Its butenyl side chain allows for interesting interactions in the synthesized proteins, making it a valuable component in the development of novel bioactive peptides.
Used in Pharmaceutical Research:
In the pharmaceutical industry, (S)-N-Fmoc-2-(3'-butenyl)alanine is used as a key component in the design and synthesis of new drug candidates. Its unique structure and properties can contribute to the development of innovative therapeutic agents with enhanced efficacy and selectivity.
Used in Materials Science:
(S)-N-Fmoc-2-(3'-butenyl)alanine can also be employed in materials science for the development of novel biomaterials and functional polymers. Its unique chemical properties and potential for interesting interactions in synthesized proteins make it a promising candidate for creating advanced materials with specific biological functions or properties.
Overall, (S)-N-Fmoc-2-(3'-butenyl)alanine is a versatile and valuable chemical compound with a wide range of applications in various fields, including peptide synthesis, pharmaceutical research, and materials science. Its unique structure and properties make it a promising building block for the development of innovative and effective solutions in these industries.

Upstream product

• 1445137-80-3 (S)-2-(benzyloxycarbonylamino)-2-methylbut-4-enoic acid 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 1011309-60-6 C₇H₁₃NO₂ 
• 84418-43-9 9-fluorenylmethyl carbamate 

Downstream Products

• 1445137-68-7 C₇₆H₁₁₄N₁₈O₁₄ 

Relevant academic research and scientific papers

Influence of α-methylation in constructing stapled peptides with olefin metathesis

Ring-closing metathesis is commonly utilized in peptide macro-cyclization. The influence of α-methylation of the amino acids bearing the olefin moieties has never been systematically studied. In this report, controlled reactions unambiguously indicate that α-methylation at the N-terminus of the metathesis sites is crucial for this reaction to occur. Also, we first elucidated that the E-isomers of stapled peptides are significantly more helical than the Z-isomers.

Design of cell-permeable stapled peptides as HIV-1 integrase inhibitors

HIV-1 integrase (IN) catalyzes the integration of viral DNA into the host genome, involving several interactions with the viral and cellular proteins. We have previously identified peptide IN inhibitors derived from the α-helical regions along the dimeric interface of HIV-1 IN. Herein, we show that appropriate hydrocarbon stapling of these peptides to stabilize their helical structure remarkably improves the cell permeability, thus allowing inhibition of the HIV-1 replication in cell culture. Furthermore, the stabilized peptides inhibit the interaction of IN with the cellular cofactor LEDGF/p75. Cellular uptake of the stapled peptide was confirmed in four different cell lines using a fluorescein-labeled analogue. Given their enhanced potency and cell permeability, these stapled peptides can serve as not only lead IN inhibitors but also prototypical biochemical probes or nanoneedles for the elucidation of HIV-1 IN dimerization and host cofactor interactions within their native cellular environment.