TAILIEUCHUNG - Báo cáo khoa học: Multifunctional host defense peptides: functional and mechanistic insights from NMR structures of potent antimicrobial peptides

The ever-increasing number of drug-resistant bacteria is a major challenge in healthcare and creates an urgent need for novel compounds for treat-ment. Host defense antimicrobial peptides have high potential to become the new generation of antibiotic compounds. Antimicrobial peptides consti-tute a major part of the innate defense system in all life forms. | ỊFEBS Journal MINIREVIEW Multifunctional host defense peptides functional and mechanistic insights from NMR structures of potent antimicrobial peptides Surajit Bhattacharjya1 and Ayyalusamy Ramamoorthy2 1 Biomolecular NMR and Drug Discovery Laboratory Schoolof BiologicalSciences Division of Structuraland ComputationalBiology Nanyang TechnologicalUniversity Singapore 2 Biophysics and Department of Chemistry University of Michigan Ann Arbor MI USA Keywords antimicrobialpeptide lipopolysaccharide LPS magainin membrane MSI NMR structure Correspondence A. Ramamoorthy Biophysics and Department of Chemistry University of Michigan Ann Arbor MI 48109-1055 USA Fax 1 734 647 4865 Tel 1 734 647 6572 E-mail ramamoor@ S. Bhattacharjya Biomolecular NMR and Drug Discovery Laboratory School of Biological Sciences Division of Structural and ComputationalBiology Nanyang TechnologicalUniversity Singapore Fax 65 6791 3856 Tel 65 6316 7997 E-mail surajit@ Received 27 April2009 revised 12 August 2009 accepted 28 August 2009 doi The ever-increasing number of drug-resistant bacteria is a major challenge in healthcare and creates an urgent need for novel compounds for treatment. Host defense antimicrobial peptides have high potential to become the new generation of antibiotic compounds. Antimicrobial peptides constitute a major part of the innate defense system in all life forms. Most of these cationic amphipathic peptides are often unstructured in isolation but readily adopt amphipathic helical structures in complex with lipid membranes. Such structural stabilization is primarily responsible for the membrane permeation and cell lysis activities of these molecules. Understanding structure-function correlations of antimicrobial peptides is critical for the development of nontoxic therapeutics. In this minireview we discuss atomic-resolution NMR structures of two highly potent helical antimicrobial peptides MSI-78 and MSI-594 providing novel

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