Designing potent antimicrobial peptides by disulphide linked dimerization and N-terminal lipidation to increase antimicrobial activity and membrane perturbation: Structural insights into lipopolysaccharide binding

Designing potent antimicrobial peptides by disulphide linked dimerization and N-terminal... Journal of Colloid and Interface Science 461 (2016) 335–345 Contents lists available at ScienceDirect Journal of Colloid and Interface Science journal homepage: www.elsevier.com/locate/jcis Designing potent antimicrobial peptides by disulphide linked dimerization and N-terminal lipidation to increase antimicrobial activity and membrane perturbation: Structural insights into lipopolysaccharide binding a b a,⇑ Aritreyee Datta , Pallob Kundu , Anirban Bhunia Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700 054, India Division of Plant Biology, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700 054, India graphical a bstract article i nfo abstract Article history: Hypothesis: The remarkable rise in multi-drug resistant Gram-negative bacterial pathogens is a major Received 24 August 2015 concern to the well being of humans as well as susceptible plants. In recent years, diseases associated Revised 14 September 2015 with inflammation and septicemia have already become a global health issue. Therefore, there is a rising Accepted 14 September 2015 demand for the development of novel ‘‘super” antibiotics. In this context, antimicrobial peptides offer an Available online 15 September 2015 attractive, alternate therapeutic solution to conventional antibiotics. Experiments: Microbroth dilution assay was performed to investigate the antimicrobial activities of the Keywords: two designed peptides against Gram http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Colloid and Interface Science Elsevier

Designing potent antimicrobial peptides by disulphide linked dimerization and N-terminal lipidation to increase antimicrobial activity and membrane perturbation: Structural insights into lipopolysaccharide binding

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Publisher
Elsevier
Copyright
Copyright © 2015 Elsevier Inc.
ISSN
0021-9797
eISSN
1095-7103
D.O.I.
10.1016/j.jcis.2015.09.036
Publisher site
See Article on Publisher Site

Abstract

Journal of Colloid and Interface Science 461 (2016) 335–345 Contents lists available at ScienceDirect Journal of Colloid and Interface Science journal homepage: www.elsevier.com/locate/jcis Designing potent antimicrobial peptides by disulphide linked dimerization and N-terminal lipidation to increase antimicrobial activity and membrane perturbation: Structural insights into lipopolysaccharide binding a b a,⇑ Aritreyee Datta , Pallob Kundu , Anirban Bhunia Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700 054, India Division of Plant Biology, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700 054, India graphical a bstract article i nfo abstract Article history: Hypothesis: The remarkable rise in multi-drug resistant Gram-negative bacterial pathogens is a major Received 24 August 2015 concern to the well being of humans as well as susceptible plants. In recent years, diseases associated Revised 14 September 2015 with inflammation and septicemia have already become a global health issue. Therefore, there is a rising Accepted 14 September 2015 demand for the development of novel ‘‘super” antibiotics. In this context, antimicrobial peptides offer an Available online 15 September 2015 attractive, alternate therapeutic solution to conventional antibiotics. Experiments: Microbroth dilution assay was performed to investigate the antimicrobial activities of the Keywords: two designed peptides against Gram

Journal

Journal of Colloid and Interface ScienceElsevier

Published: Jan 1, 2016

References

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