613675-79-9Relevant academic research and scientific papers
Condensation of α-Amino Acid with Amine in the Absence of a Coupling Agent
Yamaguchi, Jun-Ichi,Nagai, Shinya,Fukuoka, Emi,Suyama, Takayuki
, p. 830 - 831 (2007/10/03)
Treatment of N-(4-nitrophenoxycarbonyl)amino acid with an equimolar amount of amine in the absence of a coupling agent gave the corresponding α-amino acid amide in high yield.
Phosphotyrosine-containing dipeptides as high-affinity ligands for the p56(lck) SH2 domain
Llinàs-Brunet, Montse,Beaulieu, Pierre L.,Cameron, Dale R.,Ferland, Jean-Marie,Gauthier, Jean,Ghiro, Elise,Gillard, James,Gorys, Vida,Poirier, Martin,Rancourt, Jean,Wernic, Dominik,Betageri, Raj,Cardozo, Mario,Jakes, Scott,Lukas, Suzanne,Patel, Usha,Proudfoot, John,Moss, Neil
, p. 722 - 729 (2007/10/03)
Src homology-2 (SH2) domains are noncatalytic motifs containing approximately 100 amino acid residues that are involved in intracellular signal transduction. The phosphotyrosine-containing tetrapeptide Ac-pYEEI binds to the SH2 domain of p56(lck) (Lck) with an affinity of 0.1 μM. Starting from Ac-pYEEI, we have designed potent antagonists of the Lck SH2 domain which are reduced in peptidic character and in which the three carboxyl groups have been eliminated. The two C-terminal amino acids (EI) have been replaced by benzylamine derivatives and the pY + 1 glutamic acid has been substituted with leucine. The best C-terminal fragment identified, (S)-1-(4-isopropylphenyl)ethylamine, binds to the Lck SH2 domain better than the C-terminal dipeptide EI. Molecular modeling suggests that the substituents at the 4-position of the phenyl ring occupy the pY + 3 lipophilic pocket in the SH2 domain originally occupied by the isoleucine side chain. This new series of phosphotyrosine-containing dipeptides binds to the Lck SH2 domain with potencies comparable to that of tetrapeptide 1.
