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15 results on '"Suda, Srinivas"'

6. Manipulation of charged residues within the two‐peptide lantibiotic lacticin 3147

Author

Deegan, Lucy H., Suda, Srinivas, Lawton, Elaine M., Draper, Lorraine A., Hugenholtz, Floor, Peschel, Andreas, Hill, Colin, Cotter, Paul D., and Ross, R. Paul

Subjects
Lactococcus lactis, Models, Molecular, Staphylococcus aureus, Structure-Activity Relationship, Bacteriocins, Protein Conformation, Mutagenesis, Site-Directed, Microbial Sensitivity Tests, Research Articles, Anti-Bacterial Agents
Abstract

Summary Lantibiotics are antimicrobial peptides which contain a high percentage of post‐translationally modified residues. While most attention has been paid to the role of these critical structural features, evidence continues to emerge that charged amino acids also play a key role in these peptides. Here 16 ‘charge’ mutants of the two‐peptide lantibiotic lacticin 3147 [composed of Ltnα (2+, 2−) and Ltnβ (2+)] were constructed which, when supplemented with previously generated peptides, results in a total bank of 23 derivatives altered in one or more charged residues. When examined individually, in combination with a wild‐type partner or, in some instances, in combination with one another, these mutants reveal the importance of charge at specific locations within Ltnα and Ltnβ, confirm the critical role of the negatively charged glutamate residue in Ltnα and facilitate an investigation of the contribution of positively charged residues to the cationic Ltnβ. From these investigations it is also apparent that the relative importance of the overall charge of lacticin 3147 varies depending on the target bacteria and is most evident when strains with more negatively charged cell envelopes are targeted. These studies also result in, for the first time, the creation of a derivative of a lacticin 3147 peptide (LtnβR27A) which displays enhanced specific activity.

Published
2010

8. Brain Iron Homeostasis: From Molecular Mechanisms To Clinical Significance and Therapeutic Opportunities

Author

Singh, Neena, primary, Haldar, Swati, additional, Tripathi, Ajai K., additional, Horback, Katharine, additional, Wong, Joseph, additional, Sharma, Deepak, additional, Beserra, Amber, additional, Suda, Srinivas, additional, Anbalagan, Charumathi, additional, Dev, Som, additional, Mukhopadhyay, Chinmay K., additional, and Singh, Ajay, additional

Published
2014
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15. Antimicrobial Peptide Production and Purification.

Author

Suda S, Field D, and Barron N

Subjects
Antimicrobial Cationic Peptides chemistry, Antimicrobial Cationic Peptides genetics, Bacteriocins biosynthesis, Bacteriocins chemistry, Bacteriocins genetics, Bacteriocins isolation & purification, Chromatography, High Pressure Liquid methods, Disk Diffusion Antimicrobial Tests, Freeze Drying methods, Lactococcus lactis genetics, Lactococcus lactis metabolism, Mass Spectrometry methods, Nisin biosynthesis, Nisin chemistry, Nisin genetics, Nisin isolation & purification, Antimicrobial Cationic Peptides biosynthesis, Antimicrobial Cationic Peptides isolation & purification
Abstract

Antimicrobial peptides (AMPs) are natural defense compounds which are synthesized as ribosomal gene-encoded pre-peptides and produced by all living organisms. AMPs are small peptides, usually cationic and typically have hydrophobic residues which interact with cell membranes and have either a narrow or broad spectrum of biological activity. AMPs are isolated from the natural host or heterologously expressed in other hosts such as Escherichia coli. The proto-typical lantibiotic Nisin is a widely used AMP that is produced by the food-grade organism Lactococcus lactis. Although AMP production and purification procedures require optimization for individual AMPs, the Nisin production and purification protocol outlined in this chapter can be easily applied with minor modifications for the production and purification of other lantibiotics or AMPs. While Nisin is produced and secreted into the supernatant, steps to recover Nisin from both cell-free supernatant and cell pellet are outlined in detail.

Published
2017
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