142810-18-2

Usage

Uses

Given the provided materials, there are no explicit uses listed for 2-((2S,3S)-2-(((9H-fluoren-9-yl)Methoxy)carbonylaMino)-3-MethylpentanaMido)acetic acid. However, based on its structural features and potential biochemical activity, it can be hypothesized that it may find applications in various fields such as pharmaceuticals, biochemistry, or materials science. Here are some speculative uses based on its structural characteristics:
Used in Pharmaceutical Industry:
2-((2S,3S)-2-(((9H-fluoren-9-yl)Methoxy)carbonylaMino)-3-MethylpentanaMido)acetic acid could be used as a building block or a precursor in the synthesis of pharmaceutical compounds, given its structural complexity and chiral center, which may contribute to the development of novel drugs with specific therapeutic effects.
Used in Biochemical Research:
In the field of biochemistry, 2-((2S,3S)-2-(((9H-fluoren-9-yl)Methoxy)carbonylaMino)-3-MethylpentanaMido)acetic acid might be utilized as a research tool to study enzyme specificity, protein interactions, or as a probe to understand the mechanisms of biological systems, due to its structural similarity to natural amino acids and peptides.
Used in Materials Science:
2-((2S,3S)-2-(((9H-fluoren-9-yl)Methoxy)carbonylaMino)-3-MethylpentanaMido)acetic acid's unique molecular structure could also be explored in materials science for the development of new materials with specific properties, such as chiral materials or those with tailored biochemical interactions.

Upstream product

• 868-28-0 isoleucyl‐glycine 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 71989-23-6 Fmoc-Ile-OH 

Relevant academic research and scientific papers

Total stepwise solid-phase synthesis of oligonucleotide-(3'-->N)-peptide conjugates.

[structure: see text] An efficient total stepwise solid-phase synthesis of oligonucleotide-(3'-->N)-peptide conjugates is described that makes use of either a controlled pore glass support or macroporous polystyrene beads. Extending our previous homoserin

Development of designed site-directed pseudopeptide-peptido-mimetic immunogens as novel minimal subunit-vaccine candidates for malaria

Synthetic vaccines constitute the most promising tools for controlling and preventing infectious diseases. When synthetic immunogens are designed from the pathogen native sequences, these are normally poorly immunogenic and do not induce protection, as demonstrated in our research. After attempting many synthetic strategies for improving the immunogenicity properties of these sequences, the approach consisting of identifying high binding motifs present in those, and then performing specific changes on amino-acids belonging to such motifs, has proven to be a workable strategy. In addition, other strategies consisting of chemically introducing non-natural constraints to the backbone topology of the molecule and modifying the a-carbon asymmetry are becoming valuable tools to be considered in this pursuit. Non-natural structural constraints to the peptide backbone can be achieved by introducing peptide bond isosters such as reduced amides, partially retro or retro-inverso modifications or even including urea motifs. The second can be obtained by strategically replacing L-amino-acids with their enantiomeric forms for obtaining both structurally site-directed designed immunogens as potential vaccine candidates and their Ig structural molecular images, both having immunotherapeutic effects for preventing and controlling malaria.