“Supporting Information”
Synthesis, HSA-Binding and Anticancer Properties of [Cu
2( -dppm)
2(N^N)
2]
2+Bandar A. Babgi a*†, Najah A. Alzaidi a†, Jalal H. Alsayari a, Abdul-Hamid M. Emwas b, Mariusz Jaremko c, Magda H. Abdellattif d, Mostafa A. Hussien a,e
a Department of Chemistry, Faculty of Science, King Abdulaziz University, P.O. Box 80203, Jeddah 21589, Saudi Arabia.
b Core Labs, King Abdullah University of Science and Technology (KAUST), Thuwal, 23955-6900, Saudi Arabia.
c Smart-Health Initiative (SHI) and Red Sea Research Center (RSRC), Division of Biological and
Environmental Sciences and Engineering (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal, 23955-6900, Saudi Arabia.
d Chemistry Department, Deanship of Scientific Research, College of Sciences, Taif University, Al-Haweiah, P.O. Box 11099, Taif 21944, Saudi Arabia.
e Department of Chemistry, Faculty of Science, Port Said University, Port Said 42521, Egypt.
* Correspondence: [email protected]
† These authors contributed equally.
Keywords: Copper(I); bimetallic; bis(diphenylphosphino)methane; diimine; protein binding; anticancer properties.
Figure S1: 1H NMR spectrum of complex 1.
Figure S2: 31P NMR spectrum of complex 1.
Figure S3: 1H NMR spectrum of complex 2.
Figure S4: 31P NMR spectrum of complex 2.
Figure S5: 1H NMR spectrum of complex 3.
Figure S6: 31P NMR spectrum of complex 3.
353.0285 447.0512
1+
546.9478 1+
672.1090 1+
761.0400
922.10751+
NA_152_1.d: +MS, 0.2-0.4min #9-21
0.0 0.5 1.0 1.5 2.0 2.5 3.0 x106 Intens.
200 400 600 800 1000 1200 1400 1600 1800 m/z
672.10901+
673.11021+
674.10701+
675.10871+
+MS, 0.2-0.4min #9-21
672.1025 2+
672.60422+
673.1028 2+
673.6037 2+
674.10342+
674.60382+
675.10482+
C₇₄H₅₈Cu₂N₆O₄P₄, , 672.1025 0.0
0.5 1.0 1.5 2.0 2.5 x106 Intens.
0 500 1000 1500 2000
671.5 672.0 672.5 673.0 673.5 674.0 674.5 675.0 675.5 m/z
Figure S7: Mass spectrum of complex 1.
268.1002 327.06971+
447.05011+
546.9467 624.12781+
683.18511+
772.11811+ 922.10651+
NA_157_1.d: +MS, 0.2-0.3min #10-20
0.0 0.5 1.0 1.5 2.0 x106 Intens.
200 400 600 800 1000 1200 1400 1600 1800 m/z
683.1851 1+
684.1876 1+
685.18411+
686.1854 1+
+MS, 0.2-0.3min #10-20
683.1801 2+
683.68172+
684.1805 2+
684.6814 2+
685.1812 2+
685.68162+
686.18242+
C₈₂H₇₆Cu₂N₄P₄, M, 683.1801 0.0
0.5 1.0 1.5 2.0 x106 Intens.
0 500 1000 1500 2000
682.5 683.0 683.5 684.0 684.5 685.0 685.5 686.0 686.5 m/z
Figure S8: Mass spectrum of complex 2.
310.06182+
373.02551+
447.0501 1+
546.94741+
627.1132 729.1445
1+
820.07611+
931.0716 1+
1404.1207
NA_149_1.d: +MS, 0.3-0.6min #16-37
0 2 4 6 8 x105 Intens.
200 400 600 800 1000 1200 1400 1600 1800 m/z
729.1436 1+
730.1457 1+
731.1427 1+
732.1437 1+
733.1433 1+
+MS, 0.1-0.3min #3-17
729.1393 2+
729.64092+
730.13982+
730.6405 2+
731.1405 2+
731.64082+
732.1416 2+
732.6429 2+
C₈₆H₆₄Cu₂N₈P₄, M, 729.1393 0
2 4 6 x105 Intens.
0 500 1000 1500 2000
729 730 731 732 733 m/z
Figure S9: Mass spectrum of complex 3.
Figure S10: 3D illustration of complex 1 docked into HSA protein.
Figure S11: 3D illustration of complex 2 docked into HSA protein.
Figure S12: 3D illustration of complex 3 docked into HSA protein.
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