173459-80-8Relevant articles and documents
Design and synthesis of a new series of 3,5-disubstituted-1,2,4-oxadiazoles as potential colchicine binding site inhibitors: Antiproliferative activity, molecular docking, and SAR studies
Abdel-Aal, Eatedal H.,Abdel-Sami, Zakaria K.,Abo-Dya, Nader E.,Al-Karmalawy, Ahmed A.,Diab, Rana T.
, p. 21657 - 21669 (2021/12/09)
The development of anticancer compounds targeting the colchicine-binding site of tubulin, termed colchicine-binding site inhibitors (CBSIs) is a promising research area for pharmaceutical companies and research institutes. A series of 3,5-disubstituted 1,
Chemical modification of oximes with N-protected amino acids
Barbakadze, Nana N.,Jones, Rachel A.,Rosario, Nicole Rivera,Nadaraia, Nanuli Sh,Kakhabrishvili, Meri L.,Dennis Hall,Katritzky, Alan R.
, p. 7181 - 7184 (2015/02/19)
The modification of oximes, including 5α-steroids, with N-protected amino acids, in solution phase, using benzotriazole methodology is reported.
Gabapentin hybrid peptides and bioconjugates
Lebedyeva, Iryna O.,Ostrov, David A.,Neubert, John,Steel, Peter J.,Patel, Kunal,Sileno, Sean M.,Goncalves, Kevin,Ibrahim, Mohamed A.,Alamry, Khalid A.,Katritzky, Alan R.
supporting information, p. 1479 - 1486 (2014/03/21)
Synthetic approaches to gabapentin bioconjugates that overcome the tendency of gabapentin to cyclize into its γ-lactam are studied. Gabapentin was converted by N-acylation at its N-terminus into di-, tri-, and tetrapeptides (L-Ala-Gbp, L-Val-Gbp, L-Ala-L-Phe-Gbp, Gly-L-Ala-β-Ala-Gbp). Carboxyl-activated Boc-protected gabapentin was used to N-, O-, and S-acylate small peptides and hormones to give conjugates that could also provide prodrugs containing conformationally constrained gabapentin units.