210282-30-7

Usage

Uses

Used in Biochemical Research:
FMOC-L-2-NITROPHENYLALANINE is used as a spectroscopic probe for studying protein-ligand interactions and protein folding. Its incorporation into peptides allows researchers to monitor and analyze these processes in detail, providing insights into the molecular mechanisms underlying various biological functions and diseases.
Used in Peptide Synthesis:
In the field of peptide synthesis, FMOC-L-2-NITROPHENYLALANINE is used as a building block for creating novel peptide-based drug candidates. Its unique properties enable the development of therapeutic agents with specific targeting and activity profiles, contributing to the advancement of peptide-based therapeutics.
Used in Solid-Phase Peptide Synthesis:
FMOC-L-2-NITROPHENYLALANINE is employed as a key component in solid-phase peptide synthesis, a technique that allows for the stepwise assembly of peptides on an insoluble support. This method is widely used in the production of peptides and proteins, offering advantages such as ease of purification, scalability, and automation.
Used in the Development of Peptide-Based Drug Candidates:
FMOC-L-2-NITROPHENYLALANINE is used as a building block in the development of peptide-based drug candidates, enabling the creation of novel therapeutic agents with specific biological activities. Its unique chemical properties facilitate the design and synthesis of peptides with tailored pharmacological properties, potentially leading to the discovery of new treatments for various diseases.

InChI:InChI=1/C24H20N2O6/c27-23(28)21(13-15-7-1-6-12-22(15)26(30)31)25-24(29)32-14-20-18-10-4-2-8-16(18)17-9-3-5-11-19(17)20/h1-12,20-21H,13-14H2,(H,25,29)(H,27,28)/t21-/m0/s1

Upstream product

• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 1991-82-8 (2S)-2-amino-3-(2-nitrophenyl)propanoic acid 

Relevant academic research and scientific papers

Wavelength-Selective Uncaging of Two Different Photoresponsive Groups on One Effector Molecule for Light-Controlled Activation and Deactivation

Photocleavable protecting groups (PPGs) play a pivotal role in numerous studies. They enable controlled release of small effector molecules to induce biochemical function. The number of PPGs attached to a variety of effector molecules has grown rapidly in recent years satisfying the high demand for new applications. However, until now molecules carrying PPGs have been designed to activate function only in a single direction, namely the release of the effector molecule. Herein, we present the new approach Two-PPGs-One-Molecule (TPOM) that exploits the orthogonal photolysis of two photoprotecting groups to first release the effector molecule and then to modify it to suppress its induced effect. The moiety resembling the tyrosyl side chain of the translation inhibitor puromycin was synthetically modified to the photosensitive ortho-nitrophenylalanine that cyclizes upon near UV-irradiation to an inactive puromycin cinnoline derivative. Additionally, the modified puromycin analog was protected by the thio-coumarylmethyl group as the second PPG. This TPOM strategy allows an initial wavelength-selective activation followed by a second light-induced deactivation. Both photolysis processes were spectroscopically studied in the UV/vis- and IR-region. In combination with quantum-chemical calculations and time-resolved NMR spectroscopy, the photoproducts of both activation and deactivation steps upon illumination were characterized. We further probed the translation inhibition effect of the new synthesized puromycin analog upon light activation/deactivation in a cell-free GFP translation assay. TPOM as a new method for precise triggering activation/deactivation of effector molecules represents a valuable addition for the control of biological processes with light.