1445137-76-7Relevant academic research and scientific papers
Synthesis of 4-hydroxy-2-methylproline derivatives via pyrrolidine ring assembly: chromatographic resolution and diastereoselective synthesis approaches
Tiwari, Vinay Shankar,Murugula, Raghavendra,Yadav, Shyam Raj,Haq, Wahajul
, p. 865 - 871 (2016)
4-Hydroxy-2-methylproline diastereomers are successfully prepared without the use of an external chiral auxiliary. Dihydroxylation of the key intermediate 2 resulted in lactone 4 as a mixture of diastereomers in good yield. Mesylation, hydrogenation and c
Engineering strategy to improve peptide analogs: From structure-based computational design to tumor homing
Zanuy, David,Sayago, Francisco J.,Revilla-Lopez, Guillem,Ballano, Gema,Agemy, Lilach,Kotamraju, Venkata Ramana,Jimenez, Ana I.,Cativiela, Carlos,Nussinov, Ruth,Sawvel, April M.,Stucky, Galen,Ruoslahti, Erkki,Aleman, Carlos
, p. 31 - 43 (2013/04/23)
We present a chemical strategy to engineer analogs of the tumor-homing peptide CREKA (Cys-Arg-Glu-Lys-Ala), which binds to fibrin and fibrin-associated clotted plasma proteins in tumor vessels (Simberg et al. in Proc Natl Acad Sci USA 104:932-936, 2007) w
Design of cell-permeable stapled peptides as HIV-1 integrase inhibitors
Long, Ya-Qiu,Huang, Shao-Xu,Zawahir, Zahrah,Xu, Zhong-Liang,Li, Huiyuan,Sanchez, Tino W.,Zhi, Ying,De Houwer, Stephanie,Christ, Frauke,Debyser, Zeger,Neamati, Nouri
, p. 5601 - 5612 (2013/07/26)
HIV-1 integrase (IN) catalyzes the integration of viral DNA into the host genome, involving several interactions with the viral and cellular proteins. We have previously identified peptide IN inhibitors derived from the α-helical regions along the dimeric interface of HIV-1 IN. Herein, we show that appropriate hydrocarbon stapling of these peptides to stabilize their helical structure remarkably improves the cell permeability, thus allowing inhibition of the HIV-1 replication in cell culture. Furthermore, the stabilized peptides inhibit the interaction of IN with the cellular cofactor LEDGF/p75. Cellular uptake of the stapled peptide was confirmed in four different cell lines using a fluorescein-labeled analogue. Given their enhanced potency and cell permeability, these stapled peptides can serve as not only lead IN inhibitors but also prototypical biochemical probes or nanoneedles for the elucidation of HIV-1 IN dimerization and host cofactor interactions within their native cellular environment.
