caa a22 4500 445321865 CHVBK 20180317142706.0 cr unu---uuuuu 170323e20111001xx s 000 0 eng 10.1007/s10534-011-9447-0 doi (NATIONALLICENCE)springer-10.1007/s10534-011-9447-0 Antifungal activity of α-methyl trans cinnamaldehyde, its ligand and metal complexes: promising growth and ergosterol inhibitors [Elektronische Daten] [Sheikh Shreaz, Rayees Sheikh, Rimple Bhatia, Khan Neelofar, Sheikh Imran, Athar Hashmi, Nikhat Manzoor, Seemi Basir, Luqman Khan] Antifungal effectivity and utility of cinnamaldehyde is limited because of its high MIC and skin sensitivity. In this study, α-methyl trans cinnamaldehyde, a less irritating derivative, have been self coupled and complexed with Co(II) and Ni(II) to generate N, N′-Bis (α-methyl trans cinnamadehyde) ethylenediimine [C22H24N2], [Co(C44H48N4)Cl2] and [Ni(C44H48N4)Cl2]. Ligand and complexes were characterized on the basis of FTIR, ESI-MS, IR and 1HNMR techniques. Synthesized ligand [L] and complexes were investigated for their MICs, inhibition of ergosterol biosynthesis and H+ extrusion against three strains of Candida: C. albicans 44829, C. tropicalis 750 and C. krusei 6258. Average of three species MIC of methyl cinnamaldehyde is 317μg/ml (2168μM). Compared to methyl cinnamaldehyde ligand [L], Co(II) and Ni(II) complex are found to be 4.48, 17.78 and 21.46 times more effective in liquid medium and 2.73, 8.93 and 10.38 times more effective in solid medium. At their respective MIC90 average inhibition of ergosterol biosynthesis caused by methyl cinnamaldehyde, ligand [L], Co(II) and Ni(II) complex, respectively was 80, 78, 90 and 93%. H+ extrusion was also significantly inhibited but did not co-relate well with MIC90. Results indicate ergosterol biosynthesis as site of action of α-methyl cinnamaldehyde, synthesized ligand and complexes. α-methyl cinnamaldehyde and ligand did not show any toxicity against H9c2 rat cardiac myoblast cell, whereas Co(II) and Ni(II) complexes on an average produced 19% cellular toxicity. Springer Science+Business Media, LLC., 2011 Candida nationallicence α-methyl trans cinnamaldehyde nationallicence Metal complexes nationallicence PM-ATPase nationallicence Ergosterol nationallicence Shreaz Sheikh Department of Biosciences, Jamia Millia Islamia (Central University), Enzyme Kinetics Laboratory, Room NO-106, 110025, New Delhi, India aut Sheikh Rayees Department of Chemistry, Jamia Millia Islamia (Central University), 110025, New Delhi, India aut Bhatia Rimple Department of Biosciences, Jamia Millia Islamia (Central University), Enzyme Kinetics Laboratory, Room NO-106, 110025, New Delhi, India aut Neelofar Khan Department of Biosciences, Jamia Millia Islamia (Central University), Enzyme Kinetics Laboratory, Room NO-106, 110025, New Delhi, India aut Imran Sheikh Department of Applied Sciences, Jamia Millia Islamia (Central University), 110025, New Delhi, India aut Hashmi Athar Department of Chemistry, Jamia Millia Islamia (Central University), 110025, New Delhi, India aut Manzoor Nikhat Department of Biosciences, Jamia Millia Islamia (Central University), Enzyme Kinetics Laboratory, Room NO-106, 110025, New Delhi, India aut Basir Seemi Department of Biosciences, Jamia Millia Islamia (Central University), Enzyme Kinetics Laboratory, Room NO-106, 110025, New Delhi, India aut Khan Luqman Department of Biosciences, Jamia Millia Islamia (Central University), Enzyme Kinetics Laboratory, Room NO-106, 110025, New Delhi, India aut BioMetals Springer Netherlands 24/5(2011-10-01), 923-933 0966-0844 24:5<923 2011 24 10534 https://doi.org/10.1007/s10534-011-9447-0 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10534-011-9447-0 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Shreaz Sheikh Department of Biosciences, Jamia Millia Islamia (Central University), Enzyme Kinetics Laboratory, Room NO-106, 110025, New Delhi, India aut NATIONALLICENCE 700 1- Sheikh Rayees Department of Chemistry, Jamia Millia Islamia (Central University), 110025, New Delhi, India aut NATIONALLICENCE 700 1- Bhatia Rimple Department of Biosciences, Jamia Millia Islamia (Central University), Enzyme Kinetics Laboratory, Room NO-106, 110025, New Delhi, India aut NATIONALLICENCE 700 1- Neelofar Khan Department of Biosciences, Jamia Millia Islamia (Central University), Enzyme Kinetics Laboratory, Room NO-106, 110025, New Delhi, India aut NATIONALLICENCE 700 1- Imran Sheikh Department of Applied Sciences, Jamia Millia Islamia (Central University), 110025, New Delhi, India aut NATIONALLICENCE 700 1- Hashmi Athar Department of Chemistry, Jamia Millia Islamia (Central University), 110025, New Delhi, India aut NATIONALLICENCE 700 1- Manzoor Nikhat Department of Biosciences, Jamia Millia Islamia (Central University), Enzyme Kinetics Laboratory, Room NO-106, 110025, New Delhi, India aut NATIONALLICENCE 700 1- Basir Seemi Department of Biosciences, Jamia Millia Islamia (Central University), Enzyme Kinetics Laboratory, Room NO-106, 110025, New Delhi, India aut NATIONALLICENCE 700 1- Khan Luqman Department of Biosciences, Jamia Millia Islamia (Central University), Enzyme Kinetics Laboratory, Room NO-106, 110025, New Delhi, India aut NATIONALLICENCE 773 0- BioMetals Springer Netherlands 24/5(2011-10-01), 923-933 0966-0844 24:5<923 2011 24 10534 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer