LEADER 05226nam 2200649 a 450 001 9910829850203321 005 20170816114853.0 010 $a3-527-65285-X 010 $a3-527-65287-6 010 $a1-299-15730-0 010 $a3-527-65288-4 035 $a(CKB)2670000000333663 035 $a(EBL)1120589 035 $a(OCoLC)828299075 035 $a(SSID)ssj0000904705 035 $a(PQKBManifestationID)11563893 035 $a(PQKBTitleCode)TC0000904705 035 $a(PQKBWorkID)10924537 035 $a(PQKB)10931355 035 $a(MiAaPQ)EBC1120589 035 $a(PPN)178626236 035 $a(EXLCZ)992670000000333663 100 $a20130226d2013 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 10$aAntimicrobial peptides$b[electronic resource] /$fDavid A. Phoenix, Sarah R. Dennison, and Frederick Harris 210 $aWeinheim $cWiley-VCH$dc2013 215 $a1 online resource (254 p.) 300 $aDescription based upon print version of record. 311 $a3-527-33263-4 320 $aIncludes bibliographical references and index. 327 $aCover; Related Titles; Title page; Copyright page; Contents; Preface; References; List of Abbreviations; 1: Antimicrobial Peptides: Their History, Evolution, and Functional Promiscuity; Summary; 1.1 Introduction: The History of Antimicrobial Peptides; 1.2 AMPs: Evolutionarily Ancient Molecules; 1.3 AMPs: Multifunctional Molecules; 1.3.1 Defensins as Effectors of Immunity; 1.3.2 Defensins and Wound Healing; 1.3.3 Defensins and Canine Coat Color; 1.4 Discussion; References; 2: Cationic Antimicrobial Peptides; Summary; 2.1 Introduction; 2.2 CAMPs and Their Antimicrobial Action 327 $a2.3 CAMPs That Adopt an ?-Helical Structure2.4 CAMPs That Adopt a ?-Sheet Structure; 2.5 CAMPs That Adopt Extended Structures Rich in Specific Residues; 2.6 Discussion; References; 3: Anionic Antimicrobial Peptides; Summary; 3.1 Introduction; 3.2 AAMPs in the Respiratory Tract; 3.3 AAMPs in the Brain; 3.4 AAMPs in the Epidermis; 3.5 AAMPs in the Epididymis; 3.6 AAMPs in Blood Components; 3.7 AAMPs in the Gastrointestinal Tract and Food Proteins; 3.8 AAMPs and Their Structure-Function Relationships; 3.9 Discussion; References 327 $a4: Graphical Techniques to Visualize the Amphiphilic Structures of Antimicrobial PeptidesSummary; 4.1 Introduction; 4.2 Amphiphilic Structures Adopted by AMPs; 4.3 Qualitative Methods for Identifying Amphiphilic Structure; 4.4 Quantitative Techniques for Analyzing Amphiphilic Structure; 4.4.1 Techniques Based on Hydropathy Plot Analysis; 4.4.2 Techniques Based on Fourier Transforms; 4.4.3 Amphipathic Index; 4.4.4 Hydrophobic Moment Analysis; 4.4.5 Classification of Amphiphilic ?-Helices Using the Approach of Segrest; 4.4.6 Amphiphilicity Profiling Analysis of Tilted ?-Helices 327 $a4.4.7 Extended Hydrophobic Moment Plot Analysis of Tilted ?-Helices4.4.8 Amphiphilicity Quantified Using the Approach of Keller; 4.4.9 Amphiphilicity Quantified Using the Approach of Brasseur; 4.5 Discussion; References; 5: Models for the Membrane Interactions of Antimicrobial Peptides; Summary; 5.1 Introduction; 5.2 CM-Associated Factors That Affect the Antimicrobial Action of ?-CAMPs; 5.3 Mechanisms Used by CAMPs for Microbial Membrane Interaction; 5.4 Established Models for the Membrane Interactions of ?-AMPs; 5.4.1 Barrel-Stave and Toroidal Pore Models 327 $a5.4.2 Carpet Mechanism and the Shai-Huang-Matsazuki Model5.5 Recent Novel Models for the Membrane Interactions of ?-AMPs; 5.6 Tilted Peptide Mechanism; 5.7 Amyloidogenic Mechanisms; 5.8 Discussion; References; 6: Selectivity and Toxicity of Oncolytic Antimicrobial Peptides; Summary; 6.1 Introduction; 6.2 Peptide-Based Factors That Contribute to the Anticancer Action of Anticancer Peptides; 6.2.1 Sequence Length; 6.2.2 Net Positive Charge; 6.2.3 Hydrophobicity; 6.2.4 Amphiphilicity; 6.3 Membrane-Based Factors That Contribute to the Anticancer Action of ACPs; 6.3.1 Membrane Receptors 327 $a6.3.2 Cholesterol 330 $aIn this didactically-written text, the small team of expert authors presents the field in a comprehensive and accessible manner that is well suited for students and junior researchers.The result is a highly readable and systematically structured introduction to antimicrobial peptides, their structure, biological function and mode of action. The authors point the way towards a rational design of this potentially highly effective new class of clinical antibiotics on the brink of industrial application by discussing their design principles, target membranes and structure-activity relationship 606 $aPeptide antibiotics 610 0 $aMedicine--Basic Sciences. 610 0 $aPharmacy. 615 0$aPeptide antibiotics. 676 $a572.65 676 $a615/.1 700 $aPhoenix$b David A$01670866 701 $aDennison$b Sarah R$01670867 701 $aHarris$b Frederick$01670868 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910829850203321 996 $aAntimicrobial peptides$94033013 997 $aUNINA