The Science Behind N-(4-Nitrophenylsulfonyl)-L-Phenylalanine: Properties and Applications
The continuous pursuit of understanding and manipulating biological systems drives innovation in the field of chemistry, particularly in the development of specialized molecular tools. Unnatural amino acids represent a significant class of such tools, offering chemists and biologists the ability to create peptides and proteins with enhanced or entirely new functionalities. N-(4-Nitrophenylsulfonyl)-L-Phenylalanine is a notable example, distinguished by its unique chemical structure and broad applicability in research.
N-(4-Nitrophenylsulfonyl)-L-Phenylalanine is characterized by the presence of a 4-nitrophenylsulfonyl group attached to the side chain of L-phenylalanine. This modification imbues the molecule with specific optical and electronic properties. Its chemical formula is C15H14N2O6S, with a molecular weight of 350.35. Typically supplied as a white to off-white or light yellow solid, it requires careful storage conditions, such as protection from light in a dry place at temperatures between 2-8°C, to maintain its integrity and purity, which is usually specified as ≥98.0% by HPLC.
The primary applications of N-(4-Nitrophenylsulfonyl)-L-Phenylalanine stem from these unique properties. As an IR probe, it can serve as a reporter group within biomolecules, providing insights into structural changes and microenvironment variations through its distinct infrared absorption bands. This capability is invaluable in studies related to protein folding dynamics, membrane protein behavior, and ligand-protein interactions.
Equally important is its role as a FRET (Förster Resonance Energy Transfer) quencher. In FRET systems, this moiety can effectively absorb energy from a nearby fluorescent donor, thus reducing or quenching its emission. By integrating N-(4-Nitrophenylsulfonyl)-L-Phenylalanine into peptides or proteins designed for FRET assays, researchers can create sophisticated probes to study molecular proximity, binding affinities, and conformational transitions. The ability to buy high-quality peptide synthesis reagents like this is crucial for reproducible and accurate experimental outcomes.
For researchers requiring precise molecular tools, sourcing N-(4-Nitrophenylsulfonyl)-L-Phenylalanine from reputable suppliers is essential. Companies offering a range of peptide synthesis reagents and custom synthesis services are the primary sources. When evaluating where to buy, consider factors like purity guarantees, technical support, and pricing for bulk orders. The strategic use of such advanced building blocks is continually advancing our understanding of complex biological processes and paving the way for new diagnostic and therapeutic strategies.
Perspectives & Insights
Future Origin 2025
“Equally important is its role as a FRET (Förster Resonance Energy Transfer) quencher.”
Core Analyst 01
“In FRET systems, this moiety can effectively absorb energy from a nearby fluorescent donor, thus reducing or quenching its emission.”
Silicon Seeker One
“By integrating N-(4-Nitrophenylsulfonyl)-L-Phenylalanine into peptides or proteins designed for FRET assays, researchers can create sophisticated probes to study molecular proximity, binding affinities, and conformational transitions.”