abstract
A practical method for the synthesis of 2-alkyl- and 2-arylthiazolo[5,4-c]isoquinoline derivatives starting from simple commercially available reagents is presented. The recently reported La(OTf)3 catalysed reaction of dithiooxamide with 2-halobenzaldehydes to afford 2-arylthiazolo[5,4-c]isoquinolines is now extended to the synthesis of 2-alkylthiazolo[5,4-c]isoquinolines and "mixed" 2-arylthiazolo[5,4-c]isoquinolines. The new compounds can be prepared under the previously reported experimental conditions but using a 1:1 mixture of a 2halobenzaldehyde and an aliphatic or (hetero)aromatic aldehyde. The new approach also allows the access to 2alkyl-5-arylthiazolo[5,4-d]thiazoles that are hitherto unknown structures. The single-crystal X-ray diffraction structures of three thiazolo[5,4-c]isoquinolines and of two nonsymmetrical thiazolo[5,4-d]thiazoles are presented. The photophysical properties of the new thiazolo[5,4-c]isoquinoline derivatives, and their potential biological activities and toxicological risks, are discussed. Some of the new compounds show interesting bioactivity scores as kinase inhibitors.
keywords
DERIVATIVES; KINASES; RINGS
subject category
Chemistry
authors
Costa, LD; Guieu, S; Faustino, MDF; Tomé, AC
our authors
Samuel Jacques André Guieu
Junior ResearcherProjects
CICECO - Aveiro Institute of Materials (UIDB/50011/2020)
CICECO - Aveiro Institute of Materials (UIDP/50011/2020)
Collaboratory for Emerging Technologies, CoLab (EMERGING TECHNOLOGIES)
acknowledgements
This work received financial support from PT national funds (FCT/MCTES, Fundaco para a Ciencia e a Tecnologia and Ministerio da Ciencia, Tecnologia e Ensino Superior) through the projects UIDB/50006/2020, UIDP/50006/2020, UIDB/50011/2020, UIDP/50011/2020 and PTDC/QEQ-QOR/6160/2014. L. D. Costa received support from FCT/MCTES for her PhD grant SFRH/PD/BD/114578/2016. S. Guieu is supported by national funds (OE) , through FCT (Fundacao para a Ciencia e Tecnologia) for funding through program DL 57/2016 - Norma transitoria and from the Integrated Programme of SR&TD "pAGE - Protein aggregation Across the Lifespan" (reference CENTRO-01-0145-FEDER-000003) .