Contact us: +91 9550333722 040 - 40102781
Structured search
India
Choose your country
Different countries will display different contents
Try our best to find the right business for you.
My chemicalbook

Welcome back!

HomeProduct name listL-4-Cyanophenylalanine

L-4-Cyanophenylalanine

L-4-Cyanophenylalanine Structural

What is L-4-Cyanophenylalanine?

Description

p-Cyano-l-phenylalanine (pCNPhe) is an unnatural amino acid used in optical probes for imaging proteins. It was introduced in a 1994 world patent application by Richard T. Dean and co-inventors at Diatide (Londonderry, NH), who used it as a chelator for the radionuclide technetium-99m in a procedure for detecting blood clots (thrombi). The patent application was followed by a 1996 Journal of Medicinal Chemistry article.
Since that finding, pCNPhe showed its versatility in other applications. In a 2009 report, Daniel P. Raleigh, Isaac Carrico, and coauthors at the State University of New York at Stony Brook and Franklin & Marshall College (Lancaster, PA) used the molecule as a fluorescence, infrared (IR), and F?rster resonance energy transfer (FRET) probe to study protein folding, protein?membrane interactions, protein?protein interactions, and amyloid formation. They concluded that FRET, in particular, can be used directly to probe conformational changes in proteins.
In 2019, Megan C. Thielges and colleagues at Indiana University (Bloomington and Indianapolis) described the use of pCNPhe as an IR probe to characterize protein dynamics with high spatial and temporal resolution. They applied the probe at six sites in a Src1 homology 3 domain and found that their method revealed a wide range of microenvironments and distinct responses to ligand binding.
This past November, Paul S. Nerenberg, Christine M. Phillips-Piro, Scott H. Brewer, and collaborators at California State University, Los Angeles, and Franklin & Marshall once again demonstrated the utility of pCNPhe, this time as a “vibrational reporter” in the model system superfolder green fluorescent protein (sfGFP). They combined temperature-dependent IR spectroscopy, X-ray crystallography, and molecular dynamics simulations to investigate the local environment of the nitrile group in the protein. In one instance, they found that an interior site in sfGFP consists of three distinct local environments around the nitrile group, including nonspecific van der Waals interactions, hydrogen bonding to a structural water, and hydrogen bonding to a histidine side chain.
1. A proto-oncogene tyrosine–protein kinase.

The Uses of L-4-Cyanophenylalanine

4-Cyano-L-phenylalanine used as a intermediate in organic synthesis, pharmaceutical, chemical research and biochemical application.

Properties of L-4-Cyanophenylalanine

Melting point: not reported
Boiling point: 394.1±37.0 °C(Predicted)
Density  1.28±0.1 g/cm3(Predicted)
storage temp.  Keep in dark place,Sealed in dry,Store in freezer, under -20°C
solubility  100 g/l (est.)
appearance white crystals or powder
form  Solid
pka 2.13±0.10(Predicted)
Water Solubility  Slightly soluble in water.
CAS DataBase Reference 167479-78-9(CAS DataBase Reference)

Safety information for L-4-Cyanophenylalanine

Signal word Warning
Pictogram(s)
ghs
Exclamation Mark
Irritant
GHS07
GHS Hazard Statements H302:Acute toxicity,oral
H312:Acute toxicity,dermal
H332:Acute toxicity,inhalation
Precautionary Statement Codes P261:Avoid breathing dust/fume/gas/mist/vapours/spray.
P321:Specific treatment (see … on this label).
P304+P340:IF INHALED: Remove victim to fresh air and Keep at rest in a position comfortable for breathing.

Computed Descriptors for L-4-Cyanophenylalanine

Related products of tetrahydrofuran

You may like

Statement: All products displayed on this website are only used for non medical purposes such as industrial applications or scientific research, and cannot be used for clinical diagnosis or treatment of humans or animals. They are not medicinal or edible.