27220-69-5Relevant academic research and scientific papers
Mechanoenzymatic peptide and amide bond formation
Hernández, José G.,Ardila-Fierro, Karen J.,Crawford, Deborah,James, Stuart L.,Bolm, Carsten
supporting information, p. 2620 - 2625 (2017/07/17)
Mechanochemical chemoenzymatic peptide and amide bond formation catalysed by papain was studied by ball milling. Despite the high-energy mixing experienced inside the ball mill, the biocatalyst proved stable and highly efficient to catalyse the formation of α,α- and α,β-dipeptides. This strategy was further extended to the enzymatic acylation of amines by milling, and to the mechanosynthesis of a derivative of the valuable dipeptide L-alanyl-l-glutamine.
Structural studies of [2′,6′-dimethyl-L-tyrosine1]endomorphin-2 analogues: Enhanced activity and cis orientation of the Dmt-Pro amide bond
Okada, Yoshio,Fujita, Yoshio,Motoyama, Takashi,Tsuda, Yuko,Yokoi, Toshio,Li, Tingyou,Sasaki, Yusuke,Ambo, Akihiro,Jinsmaa, Yunden,Bryant, Sharon D.,Lazarus, Lawrence H.
, p. 1983 - 1994 (2007/10/03)
Analogues of endomorphin-2 (EM-2: Tyr-Pro-Phe-Phe-NH2) (1) were designed to examine the importance of each residue on μ-opioid receptor interaction. Replacement of Tyr1 by 2′,6′-dimethyl-L-tyrosine (Dmt) (9-12) exerted profound effects: [Dmt1]EM-2 (9) elevated μ-opioid affinity 4.6-fold (Kiμ=0.15 nM) yet selectivity fell 330-fold as δ-affinity rose (Kiδ=28.2 nM). This simultaneous increased μ- and δ-receptor bioactivities resulted in dual agonism (IC50=0.07 and 1.87 nM, respectively). While substitution of Phe4 by a phenethyl group (4) decreased μ affinity (Kiμ=13.3 nM), the same derivative containing Dmt (12) was comparable to EM-2 but also acquired weak δ antagonism (pA2=7.05). 1H NMR spectroscopy revealed a trans configuration (1:2 to 1:3, cis/trans) in the Tyr-Pro amide bond, but a cis configuration (5:3 to 13:7, cis/trans) with Dmt-Pro analogues.
Development of peptide 3D structure mimetics: Rational design of novel peptoid cholecystokinin receptor antagonists
Low,Black,Broughton,Buck,Davies,Dunstone,Hull,Kalindjian,McDonald,Pether,Shankley,Steel
, p. 3505 - 3517 (2007/10/03)
The two hormones cholecystokinin and gastrin share the same C-terminal sequence of amino acids, namely Gly29-Trp30-Met31-Asp32-Phe33-NH2. Nevertheless, this congruence has not precluded usi
Facile amide bond formation from esters of amino acids and peptides catalyzed by alkaline protease in anhydrous tert-butyl alcohol using ammonium chloride/triethylamine as a source of nucleophilic ammonia
Chen,Jang,Wang
, p. 858 - 860 (2007/10/02)
An industrial alkaline protease 'Alcalase', stable and active in tert-butyl alcohol, was used to catalyze the synthesis of N-protected amino acids or peptide amides in anhydrous tert-butyl alcohol using ammonium chloride/triethylamine as source of nucleophilic ammonia
