1258307-82-2Relevant articles and documents
Selective incorporation of nitrile-based infrared probes into proteins via cysteine alkylation
Jo, Hyunil,Culik, Robert M.,Korendovych, Ivan V.,Degrado, William F.,Gai, Feng
, p. 10354 - 10356 (2010)
The nitrile stretching vibration is increasingly used as a sensitive infrared probe of local protein environments. However, site-specific incorporation of a nitrile moiety into proteins is difficult. Here we show that various aromatic nitriles can be easily incorporated into peptides and proteins via either thiol alkylation or arylation reaction.
Cysteine-linked aromatic nitriles as UV resonance Raman probes of protein structure
Weeks, Colin L.,Jo, Hyunil,Kier, Brandon,De Grado, William F.,Spiro, Thomas G.
, p. 1244 - 1249 (2013/01/14)
Nitriles introduced into peptides and proteins can serve as useful vibrational spectroscopic probes, because the nitrile C≡N stretch is well isolated from backbone and sidechain vibrational bands. Aromatic nitriles offer large nC≡N absorption intensity in infrared spectra and resonance enhancement in Raman spectra with ultraviolet excitation. We report the ultraviolet resonance Raman spectra of cyanophenylalanine attached to cysteine, through linkage reactions that are applicable to cysteine residues in proteins. Excitation profiles are reported, and the nC≡N detection limit is estimated to be 5μM. The band position is sensitive to solvent polarity and especially to strong H-bonding. The derivatization of mastoparan X peptide at introduced cysteine residues demonstrated the effectiveness of a cyanophenylcysteine probe in reporting the lowered environmental polarity when the peptide was incorporated into liposomes. For an asymmetrical cyanophenyl derivative, 2-CBCys, the intensity ratio of asymmetric and symmetric ring modes, n8b and n8a, was found to respond to solvent polarity and not to H-bonding. 2012 John Wiley & Sons, Ltd.
