122092-18-6Relevant articles and documents
Spectrophotometric study on the thermodynamics of binding of α- and β-cyclodextrin towards some p-nitrobenzene derivatives
Meo, Paolo Lo,D'Anna, Francesca,Riela, Serena,Gruttadauria, Michelangelo,Noto, Renato
, p. 1584 - 1590 (2003)
Binding properties of native α- and β-cyclodextrin towards some nitrobenzene derivatives have been studied by means of UV-vis spectrophotometry. The former host is able to form complexes having 1 : 1 and 1 : 2 stoichiometric ratios with these guests, whil
Amino-acid-functionalized solvatochromic probes
Schreiter, Katja,Spange, Stefan
, p. 242 - 250 (2008/09/20)
N-(4-nitrophenyl)-L-proline (2) has been obtained by a nucleophilic aromatic substitution reaction of 4-fluoronitrobenzene with L-proline. The corresponding amide derivatives 3-5 have been synthesized by peptide coupling of 2 with different amino acid derivatives and chiral amines. Solvatochromism of the long-wavelength UV/Vis band in the electronic absorption spectra of the compounds 2-5 has been studied and analyzed using the empirical Kamlet-Taft solvent polarity parameters π* (dipolarity/polarizability), α (hydrogen bond donating ability), and β (hydrogen bond accepting ability). Reasonable Kamlet-Taft solvatochromic correlations (r > 0.95) were established for the three amide derivatives 3-5 in a range of common solvents and three room temperature ionic liquids (RTILs). The UV/Vis absorption of the 4-nitroaniline derivative 2 showed a hypsochromic shift with increasing concentration due to intermolecular hydrogen bonded aggregate formation in protic solvents, which is not observed for compounds 3-5. Copyright 2008 John Wiley & Sons, Ltd.
N-aryl-prolyl-dipeptides as potent antagonists of VLA-4.
Kamenecka, Theodore M,Lanza Jr., Thomas,de Laszlo, Stephen E,Li, Bing,McCauley, Ermengilda D,Van Riper, Gail,Egger, Linda A,Kidambi, Usha,Mumford, Richard A,Tong, Sharon,MacCoss, Malcolm,Schmidt, John A,Hagmann, William K
, p. 2205 - 2208 (2007/10/03)
The design, synthesis, and biological evaluation of N-arylprolyl-dipeptide derivatives as small molecule VLA-4 antagonists is described. Potency against VLA-4 and alpha(4)beta(7) and rat pharmacokinetic evaluation revealed some advantages over the related N-(arylsulfonyl)-prolyl-dipeptide analogues.