Antimicrobial peptides [[electronic resource] /] / David A. Phoenix, Sarah R. Dennison, and Frederick Harris

• Autore: Phoenix David A
• Pubblicazione: Weinheim, : Wiley-VCH, c2013
• Descrizione fisica: 1 online resource (254 p.)
• Disciplina: 572.65; 615/.1
• Soggetto topico: Peptide antibiotics
• Soggetto non controllato: Medicine--Basic Sciences; Pharmacy
• Altri autori: DennisonSarah R HarrisFrederick
• Note generali: Description based upon print version of record.
• Nota di bibliografia: Includes bibliographical references and index.
• Nota di contenuto: Cover; 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 ; 2.3 CAMPs That Adopt an α-Helical Structure2.4 CAMPs That Adopt a β-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 ; 4: 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 α-Helices Using the Approach of Segrest; 4.4.6 Amphiphilicity Profiling Analysis of Tilted α-Helices ; 4.4.7 Extended Hydrophobic Moment Plot Analysis of Tilted α-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 α-CAMPs; 5.3 Mechanisms Used by CAMPs for Microbial Membrane Interaction; 5.4 Established Models for the Membrane Interactions of α-AMPs; 5.4.1 Barrel-Stave and Toroidal Pore Models ; 5.4.2 Carpet Mechanism and the Shai-Huang-Matsazuki Model5.5 Recent Novel Models for the Membrane Interactions of α-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 ; 6.3.2 Cholesterol
• Sommario/riassunto: In 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
• Titolo autorizzato: Antimicrobial peptides
• ISBN: 3-527-65285-X; 3-527-65287-6; 1-299-15730-0; 3-527-65288-4
• Formato: Materiale a stampa
• Livello bibliografico: Monografia
• Lingua di pubblicazione: Inglese
• Record Nr.: 9910829850203321
• Lo trovi qui: Univ. Federico II