Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/57414
Title: Structural studies of antimicrobial peptides by nuclear magnetic resonance (NMR) spectroscopy: mechanistic insights towards structure-function correlations.
Authors: Rathi Saravanan
Keywords: DRNTU::Science::Biological sciences
Issue Date: 2011
Abstract: Prolonged antibiotic misusage in human therapeutics, agriculture and veterinary, has favored the survival and spread of antibiotic resistant bacteria termed as multi drug resistant (MDR) bacteria or "superbugs". With death due to bacterial infections being ranked 4th leading cause in the U.S, treatment to such bacterial infections has become a serious concern to public health. Septicemia or commonly referred sepsis is the 10th leading cause of death in U.S with over 700,000 cases of severe sepsis estimated to occur every year. Sepsis is defined as the clinical conditions caused by host immune response to the bacterial infection characterized by systemic inflammation and coagulation. In scenario of the MDR pathogens, sepsis has emerged as the most common cause of death in intensive care units worldwide. Lipopolysaacharide (LPS) or endotoxin, the major component of the outer membrane of Gram-negative bacteria essential for bacterial survival is the key "pathogen associated molecule" causing sepsis. Endotoxin released into blood stream, during a Gram-negative bacterial infection acts as a key stimulator of host innate immune response. An uncontrolled stimulation of such response may cause overwhelmed production of inflammatory cytokines like TNF, IL-6 leading to hemorrhage and organ dysfunction termed as sepsis /septic shock. The ever increasing prevalence of "superbugs" and growing population of immune compromised patients with clinical conditions like sepsis, leukemia, hematopoietic defects etc, demands urgent need for the development of therapeutic alternatives to conventional antibiotics. Over the past few decades, a search for novel antibiotics has led to identification of cationic peptides with antimicrobial activity.
Description: 248 p.
URI: http://hdl.handle.net/10356/57414
Rights: Nanyang Technological University
Fulltext Permission: restricted
Fulltext Availability: With Fulltext
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