1234782-72-9Relevant academic research and scientific papers
Solution-phase submonomer diversification of aza-dipeptide building blocks and their application in aza-peptide and aza-DKP synthesis
Bourguet, Carine B.,Proulx, Caroline,Klocek, Sophie,Sabatino, David,Lubell, William D.
, p. 284 - 296 (2010)
Aza-peptides have been used as tools for studying SARs in programs aimed at drug discovery and chemical biology. Protected aza-dipeptides were synthesized by a solution-phase submonomer approach featuring alkylation of N-terminal benzophenone semicarbazon
Paired Utility of Aza-Amino Acyl Proline and Indolizidinone Amino Acid Residues for Peptide Mimicry: Conception of Prostaglandin F2α Receptor Allosteric Modulators That Delay Preterm Birth
Mir, Fatemeh M.,Atmuri, N. D. Prasad,Bourguet, Carine B.,Fores, Jennifer Rodon,Hou, Xin,Chemtob, Sylvain,Lubell, William D.
, p. 4500 - 4525 (2019/05/17)
Peptide mimicry employing a combination of aza-amino acyl proline and indolizidinone residues has been used to develop allosteric modulators of the prostaglandin F2α receptor. The systematic study of the N-terminal phenylacetyl moiety and the conformation and side chain functions of the central turn dipeptide residue has demonstrated the sensitive relationships between modulator activity and topology. Examination of aza-Gly-Pro and aza-Phe-Pro analogs 2a and 2b in a murine preterm labor model featuring treatment with lipopolysaccharide demonstrated their capacity to extend significantly (>20 h) the average time of delivery offering new prototypes for delaying premature birth.
Design and synthesis of novel azapeptide activators of apoptosis mediated by caspase-9 in cancer cells
Bourguet, Carine B.,Boulay, Pierre-Luc,Claing, Audrey,Lubell, William D.
, p. 3361 - 3365 (2014/07/22)
A set of azapeptides was designed based on the Ala-Val-Pro-Ile peptide (derived from Smac protein) to activate caspase-9 and induce apoptosis in breast cancer cells. The diversity-oriented synthesis of the aza-peptides 5-9 was accomplished by alkylation o
