102422-45-7Relevant articles and documents
Mechanochemical Preparation of 3,5-Disubstituted Hydantoins from Dipeptides and Unsymmetrical Ureas of Amino Acid Derivatives
Konnert, Laure,Gonnet, Lori,Halasz, Ivan,Suppo, Jean-Simon,De Figueiredo, Renata Marcia,Campagne, Jean-Marc,Lamaty, Fredéric,Martinez, Jean,Colacino, Evelina
, p. 9802 - 9809 (2016)
5-Substituted-3-(alkoxycarbonyl)alkyl-hydantoin derivatives were prepared by mechanochemistry from amino esters or dipeptides, via a 1,1′-carbonyldiimidazole-mediated one-pot/two-step cyclization reaction involving amino acid unsymmetrical urea A and carboxy-imidazolyl-dipeptide ester B intermediates. Comparative experiments in solution were also performed. The successful preparation of an antibacterial agent precursor was also investigated.
Poly(ethylene glycol)s as grinding additives in the mechanochemical preparation of highly functionalized 3,5-disubstituted hydantoins
Mascitti, Andrea,Lupacchini, Massimiliano,Guerra, Ruben,Taydakov, Ilya,Tonucci, Lucia,D'Alessandro, Nicola,Lamaty, Frederic,Martinez, Jean,Colacino, Evelina
, p. 19 - 25 (2017)
The mechanochemical preparation of highly functionalized 3,5-disubstituted hydantoins was investigated in the presence of various poly(ethylene) glycols (PEGs), as safe grinding assisting agents (liquid-assisted grinding, LAG). A comparative study under drygrinding conditions was also performed. The results showed that the cyclization reaction was influenced by the amount of the PEG grinding agents. In general, cleaner reaction profiles were observed in the presence of PEGs, compared to dry-grinding procedures.
Benzotriazole-mediated synthesis of aza-peptides: En route to an aza-leuenkephalin analogue
Abo-Dya, Nader E.,Biswas, Suvendu,Basak, Akash,Avan, Ilker,Alamry, Khalid A.,Katritzky, Alan R.
, p. 3541 - 3552 (2013/05/23)
Novel N-(N-Pg-azadipeptidoyl)benzotriazoles 20a-e couple efficiently with α-amino acids 21a-e, dipeptides 22a-c, aminoxyacetic acid 23a, depsidipeptide 23b, and α-hydroxy-β-phenylpropionic acid 27 yielding, respectively, azatripeptides 24a-g, azatetrapeptides 25a,b, a hybrid azatripeptide with an oxyamide bond 26a, a hybrid azatetrapeptide with an ester bond 26b, and a hybrid azatripeptide with an ester bond 28. A new protocol for the synthesis of N-Pg-azatripeptides 33a,b and 35a,b, each containing a natural amino acid at the N-terminus, avoids the low coupling rates of the aza-amino acid residue and enables the solution-phase synthesis of an azaphenylalanine analogue of Leu-enkephalin 40.
Oxyazapeptides: Synthesis, structure determination, and conformational analysis
Biswas, Suvendu,Abo-Dya, Nader E.,Oliferenko, Alexander,Khiabani, Amir,Steel, Peter J.,Alamry, Khalid A.,Katritzky, Alan R.
, p. 8502 - 8509 (2013/09/24)
Herein we report the synthesis, X-ray structure determination, and conformational analysis of a novel class of heteroatom-modified peptidomimetics, which we shall call "oxyazapeptides". Substituting the typical native N-Cα bond with an O-Nα bond creates a completely new, previously unknown family of peptidomimetics, which are hydrolytically stable and display very interesting conformational behavior. Force field calculations revealed that the barrier to rotation around the O-Nα bond in oxyazapeptides is five times lower than that around the N-Nα bond in azapeptides. Also, conformational analysis supported by X-ray suggests that the oxyaza moiety can effectively induce β-turns, which can make the newly discovered oxyazapeptide scaffold a useful tool for drug discovery and for design of biologics.
N, N'-carbonyldiimidazole-mediated DBU-catalyzed one-pot synthesis of urea-tethered glycosyl amino acids and glycoconjugates
Sureshbabu,Basavaprabhu
experimental part, p. 1160 - 1164 (2011/07/09)
An efficient, mild, simple, and alternative one-pot protocol for the synthesis of urea-tethered glycosyl amino acids mediated by N,N'- carbonyldiimidazole employing DBU as a catalyst is described. This protocol is also extended for the synthesis of urea-tethered disaccharides and oligosaccharides. Georg Thieme Verlag Stuttgart - New York.
Inactivation of Leukocyte Elastase by Aryl Azolides and Sulfonate Salts. Structure-Activity Relationship Studies
Groutas, W. C.,Brubaker, M. J.,Zandler, M. E.,Mazo-Gray, V.,Rude, S. A.,et al.
, p. 1302 - 1305 (2007/10/02)
The inhibitory activity of a series of aryl azolides and sulfonate salts toward human leukocyte elastase is reported.Several of the compounds were found to be potent inhibitors of the enzyme.Active compounds were obtained only when the specificity group and the reactive moiety were separated by a two-carbon chain.The introduction of hydrophobic groups enhanced the inhibitory activity of these compounds, with the exception of the sulfonate salts.The nature of the leaving group had had a profound effect on inhibitory activity, with compounds 23 and 26 being the most active (kobsd/ = 11722 and 13500 M-1 s-1, respectively).
