ABSTRACT
Background: Tigecycline is the first commercially available glycycline, derivatives of the tetracycline antibiotics, having enhanced activity against various pathogens. In vitro activity has been demonstrated against multi drug resistant Gram positive and Gram negative pathogens like MRSA, ESBL producing Esch.coli and Klebsiella spp. and Acinetobacter Objective: To determine Tigecycline in vitro susceptibility pattern in MRSA, ESBL producing Esch.coli and Klebsiella spp. and Acinetobacter spp. Material and Methods: Investigations were carried out from August 2012-January 2014 to detect MRSA,ESBL producing Escherichia coli and Klebsiella spp. as well as Acinetobacter spp. by using a standard protocols and Tigecycline in-vitro susceptibility testing was done by Kirby Bauer Disc diffusion method and it’s MIC value against resistant isolates was evaluated.Statistical analysis was done by Fishers extract method. Result: Out of 107 Staphylococcus aureus isolates 52(48.59%) were MRSA, none of them showed resistance to Tigecycline. Out of 82 Esch.coli isolates 14 (i.e 17.07%) were ESBL producers, none of them showed resistance to Tigecycline.Out of 67 Klebsiella isolates 21 (i.e 31.34%) were ESBL producers out of which only 1 (i.e 4.76%) was resistant to Tigecycline.Out of 19 Acinetobacter spp.isolated 3 (i.e 15.78%) were resistant to Tigecycline. The MIC range for ESBL producing Eschcoli, Klebsiella spp., MRSA and acinetobacter spp were 0.14-0.45 μg/ml,0.25-2.4 μg/ml,0.12-0.26 μg/ml, 1-3.2 μg/ml respectively. Conclusion: The results of the study confirm the excellent in vitro activity of Tigecycline against Gram positive and Gram negative multidrug resistant pathogens.
ABSTRACT
The circular dichroic spectra of a-globulin from Sesamum indicum L. was recorded in the presence of cetyltrimethyl ammonium bromide, Triton X-100 and Brij-36T. The protein in 0.2 Μ phosphate buffer pH 7.4 had about 25% β-structure and 5% α-helix, the rest being aperiodic or irregular structure and a-helix, structure was increased by cationic detergent cetyl trimethyl ammonium bromide. But, the increase in α-helix content was much less than that induced by an anionic detergent, sodium dodecyl sulphate. In non-ionic detergent like Brij-36T and Triton X-100, specific β-structures like II-β and I-β were formed along with changes in α-helical and aperiodic structures. These results suggest that the protein has a fairly labile quaternary structure.