Antimicrobial peptides [[electronic resource] /] / David A. Phoenix, Sarah R. Dennison, and Frederick Harris |
Autore | Phoenix David A |
Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2013 |
Descrizione fisica | 1 online resource (254 p.) |
Disciplina |
572.65
615/.1 |
Altri autori (Persone) |
DennisonSarah R
HarrisFrederick |
Soggetto topico | Peptide antibiotics |
Soggetto non controllato |
Medicine--Basic Sciences
Pharmacy |
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 | eng |
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 |
Record Nr. | UNINA-9910141488903321 |
Phoenix David A | ||
Weinheim, : Wiley-VCH, c2013 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Antimicrobial peptides [[electronic resource] /] / David A. Phoenix, Sarah R. Dennison, and Frederick Harris |
Autore | Phoenix David A |
Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2013 |
Descrizione fisica | 1 online resource (254 p.) |
Disciplina |
572.65
615/.1 |
Altri autori (Persone) |
DennisonSarah R
HarrisFrederick |
Soggetto topico | Peptide antibiotics |
Soggetto non controllato |
Medicine--Basic Sciences
Pharmacy |
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 | eng |
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 |
Record Nr. | UNINA-9910829850203321 |
Phoenix David A | ||
Weinheim, : Wiley-VCH, c2013 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Antimicrobial peptides / / David A. Phoenix, Sarah R. Dennison, and Frederick Harris |
Autore | Phoenix David A |
Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2013 |
Descrizione fisica | 1 online resource (254 p.) |
Disciplina |
572.65
615/.1 |
Altri autori (Persone) |
DennisonSarah R
HarrisFrederick |
Soggetto topico | Peptide antibiotics |
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 | eng |
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 |
Record Nr. | UNINA-9910876672703321 |
Phoenix David A | ||
Weinheim, : Wiley-VCH, c2013 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Novel antimicrobial agents and strategies / / edited by David A. Phoenix, Frederick Harris and Sarah R. Dennison ; contributors Waqar Ahmed [and thirty one others] |
Pubbl/distr/stampa | Weinheim, Germany : , : Wiley-VCH, , 2015 |
Descrizione fisica | 1 online resource (439 p.) |
Disciplina | 614.48 |
Soggetto topico |
Disinfection and disinfectants
Anti-infective agents Sterilization |
ISBN |
3-527-67615-5
3-527-67613-9 3-527-67614-7 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Novel Antimicrobial Agents and Strategies; Contents; List of Contributors; Preface; Chapter 1 The Problem of Microbial Drug Resistance; 1.1 Introduction; 1.2 History of the Origins, Development, and Use of Conventional Antibiotics; 1.3 Problems of Antibiotic Resistance; 1.4 Multiple Drug-Resistant (MDR), Extensively Drug-Resistant (XDR), and Pan-Drug-Resistant (PDR) Organisms; 1.5 MDR Mechanisms of Major Pathogens; 1.6 Antimicrobial Stewardship Programs; 1.7 Discussion; Acknowledgment; References; Chapter 2 Conventional Antibiotics -- Revitalized by New Agents; 2.1 Introduction
2.2 Conventional Antibiotics2.3 The Principles of Combination Antibiotic Therapy; 2.4 Antibiotic Resistance Breakers: Revitalize Conventional Antibiotics; 2.4.1 β-Lactamase Inhibitors; 2.4.2 Aminoglycoside-Modifying Enzyme Inhibitors; 2.4.3 Antibiotic Efflux Pumps Inhibitors; 2.4.4 Synergy Associated with Bacterial Membrane Permeators; 2.5 Discussion; Acknowledgments; References; Chapter 3 Developing Novel Bacterial Targets: Carbonic Anhydrases as Antibacterial Drug Targets; 3.1 Introduction; 3.2 Carbonic Anhydrases; 3.3 CA Inhibitors; 3.4 Classes of CAs Present in Bacteria 3.5 Pathogenic Bacterial CAs3.6 α-CAs in Pathogenic Bacteria; 3.7 β-CAs in Pathogenic Bacteria; 3.8 γ-CAs from Pathogenic Bacteria; 3.9 Conclusions; References; Chapter 4 Magainins -- A Model for Development of Eukaryotic Antimicrobial Peptides (AMPs); 4.1 Introduction; 4.2 Magainins and Their Antimicrobial Action; 4.3 Magainins as Antibiotics; 4.4 Other Antimicrobial Uses of Magainins; 4.5 Future Prospects for Magainins; References; Chapter 5 Antimicrobial Peptides from Prokaryotes; 5.1 Introduction; 5.2 Bacteriocins; 5.2.1 Microcins -- Peptide Bacteriocins from Gram-Negative Bacteria 5.2.2 Lanthibiotics -- Post-translationally Modified Peptides from Gram-Positive Bacteria5.2.3 Non-modified Peptides from Gram-Positive Bacteria; 5.3 Applications of Prokaryotic AMPs; 5.3.1 Food Biopreservation; 5.3.2 Bacteriocinogenic Probiotics; 5.3.3 Clinical Application; 5.3.4 Applications in Dental Care; 5.4 Development and Discovery of Novel AMP; References; Chapter 6 Peptidomimetics as Antimicrobial Agents; 6.1 Introduction; 6.2 Antimicrobial Peptidomimetics; 6.2.1 Peptoids; 6.2.2 β-Peptides; 6.2.3 Arylamides; 6.2.4 β-Peptoid--Peptide Hybrid Oligomers 6.2.5 Oligourea and γ 4-Peptide-Based Oligomers6.2.6 AApeptides; 6.2.6.1 α-AApeptides; 6.2.6.2 γ-AApeptides; 6.3 Discussion; Acknowledgments; References; Chapter 7 Synthetic Biology and Therapies for Infectious Diseases; 7.1 Current Challenges in the Treatment of Infectious Diseases; 7.2 Introduction to Synthetic Biology; 7.3 Vaccinology; 7.3.1 Genetic Engineering and Vaccine Development; 7.3.2 Rational Antigen Design Through Reverse Vaccinology; 7.4 Bacteriophages: A Re-emerging Solution?; 7.4.1 A Brief History of Bacteriophages 7.4.2 Addressing the Problem of the Restricted Host Range of Phages |
Record Nr. | UNINA-9910132344003321 |
Weinheim, Germany : , : Wiley-VCH, , 2015 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Novel antimicrobial agents and strategies / / edited by David A. Phoenix, Frederick Harris and Sarah R. Dennison ; contributors Waqar Ahmed [and thirty one others] |
Pubbl/distr/stampa | Weinheim, Germany : , : Wiley-VCH, , 2015 |
Descrizione fisica | 1 online resource (439 p.) |
Disciplina | 614.48 |
Soggetto topico |
Disinfection and disinfectants
Anti-infective agents Sterilization |
ISBN |
3-527-67615-5
3-527-67613-9 3-527-67614-7 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Novel Antimicrobial Agents and Strategies; Contents; List of Contributors; Preface; Chapter 1 The Problem of Microbial Drug Resistance; 1.1 Introduction; 1.2 History of the Origins, Development, and Use of Conventional Antibiotics; 1.3 Problems of Antibiotic Resistance; 1.4 Multiple Drug-Resistant (MDR), Extensively Drug-Resistant (XDR), and Pan-Drug-Resistant (PDR) Organisms; 1.5 MDR Mechanisms of Major Pathogens; 1.6 Antimicrobial Stewardship Programs; 1.7 Discussion; Acknowledgment; References; Chapter 2 Conventional Antibiotics -- Revitalized by New Agents; 2.1 Introduction
2.2 Conventional Antibiotics2.3 The Principles of Combination Antibiotic Therapy; 2.4 Antibiotic Resistance Breakers: Revitalize Conventional Antibiotics; 2.4.1 β-Lactamase Inhibitors; 2.4.2 Aminoglycoside-Modifying Enzyme Inhibitors; 2.4.3 Antibiotic Efflux Pumps Inhibitors; 2.4.4 Synergy Associated with Bacterial Membrane Permeators; 2.5 Discussion; Acknowledgments; References; Chapter 3 Developing Novel Bacterial Targets: Carbonic Anhydrases as Antibacterial Drug Targets; 3.1 Introduction; 3.2 Carbonic Anhydrases; 3.3 CA Inhibitors; 3.4 Classes of CAs Present in Bacteria 3.5 Pathogenic Bacterial CAs3.6 α-CAs in Pathogenic Bacteria; 3.7 β-CAs in Pathogenic Bacteria; 3.8 γ-CAs from Pathogenic Bacteria; 3.9 Conclusions; References; Chapter 4 Magainins -- A Model for Development of Eukaryotic Antimicrobial Peptides (AMPs); 4.1 Introduction; 4.2 Magainins and Their Antimicrobial Action; 4.3 Magainins as Antibiotics; 4.4 Other Antimicrobial Uses of Magainins; 4.5 Future Prospects for Magainins; References; Chapter 5 Antimicrobial Peptides from Prokaryotes; 5.1 Introduction; 5.2 Bacteriocins; 5.2.1 Microcins -- Peptide Bacteriocins from Gram-Negative Bacteria 5.2.2 Lanthibiotics -- Post-translationally Modified Peptides from Gram-Positive Bacteria5.2.3 Non-modified Peptides from Gram-Positive Bacteria; 5.3 Applications of Prokaryotic AMPs; 5.3.1 Food Biopreservation; 5.3.2 Bacteriocinogenic Probiotics; 5.3.3 Clinical Application; 5.3.4 Applications in Dental Care; 5.4 Development and Discovery of Novel AMP; References; Chapter 6 Peptidomimetics as Antimicrobial Agents; 6.1 Introduction; 6.2 Antimicrobial Peptidomimetics; 6.2.1 Peptoids; 6.2.2 β-Peptides; 6.2.3 Arylamides; 6.2.4 β-Peptoid--Peptide Hybrid Oligomers 6.2.5 Oligourea and γ 4-Peptide-Based Oligomers6.2.6 AApeptides; 6.2.6.1 α-AApeptides; 6.2.6.2 γ-AApeptides; 6.3 Discussion; Acknowledgments; References; Chapter 7 Synthetic Biology and Therapies for Infectious Diseases; 7.1 Current Challenges in the Treatment of Infectious Diseases; 7.2 Introduction to Synthetic Biology; 7.3 Vaccinology; 7.3.1 Genetic Engineering and Vaccine Development; 7.3.2 Rational Antigen Design Through Reverse Vaccinology; 7.4 Bacteriophages: A Re-emerging Solution?; 7.4.1 A Brief History of Bacteriophages 7.4.2 Addressing the Problem of the Restricted Host Range of Phages |
Record Nr. | UNINA-9910817868703321 |
Weinheim, Germany : , : Wiley-VCH, , 2015 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|