Studies on the structure-function relationships of membrane-active segments derived from pore forming toxin and anti-microbial peptides
IR@CDRI: CSIR-Central Drug Research Institute, Lucknow
View Archive Info| Field | Value | |
| Creator |
Pandey, B K
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| Date |
2014-05-19T12:06:47Z
2014-05-19T12:06:47Z 2010 |
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| Identifier |
http://hdl.handle.net/123456789/1249
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| Description |
Guide- Dr. Jimut Kanti Ghosh, PhD. Thesis Submitted to JNU, New Delhi in 2010.
Scientific community is well aware of the fact that pathogenic microorganisms are becoming resistant to conventional antibiotics at a fast pace. To circumvent this problem, efforts are now directed towards those molecules which can escape the mechanism of pathogenic resistance. Antimicrobial peptides are one such group of molecule which has been serving the purpose of nature’s antibiotic throughout the evolution. In many organisms they act as a first line of defense against invading microorganisms. However, their utilization to combat infection outside their natural host requires precise understanding of their mechanism of action due to their display of toxicity towards mammalian cells in vitro. Understanding their mechanism of action will assist in design of novel antimicrobial peptide based therapeutics with cell selective activities as well as resistance to antibiotic resistant pathogens. Therefore this work is focused towards identification of those factors which impart toxicity to antimicrobial peptides. This has been done by selective mutation in the sequence of melittin, magainin 2 and bombolitin V. Introductory Chapter 1 presents a brief background of the present work alongwith the objectives and rationale. Chapter 2 reviews the available literature on antimicrobial peptides. Chapter 3 describes the materials and methods used to carry out the investigations. Outcome of our investigation on effect of leucine zipper motif on biological activity of melittin and its synthetic analogs is presented in Chapter 4. Chapter 5 deals with the conversion of a non-toxic molecule magainin 2 into toxic one by introduction of a leucine zipper motif into its sequence. Finally Chapter 6 discusses the regulation of toxicity in bombolitin V by mutation in a conserved leucine zipper motif, it also present the design of a bombolitin V analog having significantly improved antimicrobial activity with simultaneous reduction of toxicity. |
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3846919 bytes
application/pdf |
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| Language |
en
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| Relation |
CSIR-CDRI Thesis No. - P-51
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| Subject |
Membrane-active segments
Toxin Anti-microbial peptides |
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| Title |
Studies on the structure-function relationships of membrane-active segments derived from pore forming toxin and anti-microbial peptides
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| Type |
Thesis
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