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Peptide and protein desiegn for biopharmaceutical applications / / editor, Knud J. Jensen
| Peptide and protein desiegn for biopharmaceutical applications / / editor, Knud J. Jensen |
| Pubbl/distr/stampa | West Sussex, UK ; ; Hoboken, NJ, : Wiley, 2009 |
| Descrizione fisica | 1 online resource (314 p.) |
| Disciplina | 615/.19 |
| Altri autori (Persone) | JensenKnud J |
| Soggetto topico |
Peptide drugs - Design
Protein drugs - Design Peptides - Design Protein engineering |
| ISBN |
1-282-29176-9
9786612291760 0-470-74971-7 0-470-74970-9 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Peptide and Protein Design for Biopharmaceutical Applications; Contents; List of Contributors; Preface; 1 Introduction; 2 Computational Approaches in Peptide and Protein Design: An Overview; 2.1 Introduction; 2.2 Basics and Tools; 2.2.1 The Importance of Computational Approaches; 2.2.2 Tools and Procedures: Force Fields and Sampling; 2.3 Computational Study of Cyclopentapeptide Inhibitors of CXCR4; 2.3.1 The 3D Pharmacophore Model for FC131; 2.3.2 A 3D Model of the TM Region of CXCR4; 2.3.3 Docking of FC131 to CXCR4; Acknowledgements; References; 3 Aspects of Peptidomimetics; 3.1 Introduction
3.2 Modified Peptides3.3 Pseudopeptides; 3.4 Secondary Structure Mimics (Excluding Turn Mimics); 3.4.1 -strand Mimetics; 3.4.2 Helix Mimetics; 3.5 Examples of Peptidomimetics; 3.6 Conclusion; References; 4 Design of Cyclic Peptides; 4.1 Introduction; 4.1.1 Pharmaceutical Research Today; 4.1.2 General Advantages of Cyclic Peptide Structures; 4.1.3 Examples of Cyclic Peptides of Medicinal Interest; 4.1.4 General Considerations; 4.2 Peptide Cyclization; 4.2.1 Possibilities of Peptide Cyclization; 4.2.2 Synthesis of Cyclic Peptides; 4.2.3 Chemical Modifications of Cyclic Peptides 4.2.4 Concluding Remarks4.3 Conformation and Dynamics of Cyclic Peptides; 4.3.1 Reductions in Conformational Space; 4.3.2 Conformational Arrangements in Cyclic Structures; 4.3.3 Flexibility of Cyclized Scaffolds; 4.3.4 Experimental Structure Characterization; 4.4 Concepts in the Rational Design of Cyclic Peptides; 4.4.1 The Influence of Amino Acid Composition; 4.4.2 The Dunitz-Waser Concept; 4.4.3 The Spatial Screening Technique; 4.4.4 General Strategy for Finding Active Hits; 4.5 Examples of Cyclic Peptides as Drug Candidates; 4.5.1 Cilengitide as Integrin Inhibitor; 4.5.2 CXCR4 Antagonists 4.5.3 Sandostatin and the Veber-Hirschmann Peptide as Examples of Rational Design4.6 Conclusion; References; 5 Carbohydrates in Peptide and Protein Design; 5.1 Introduction; 5.2 Configurational and Conformational Properties of Carbohydrates; 5.3 Carbohydrates in Peptidomimetics; 5.4 Glycopeptides; 5.5 Carbohydrates as Scaffolds in the Design of Nonpeptide Peptidomimetics; 5.6 Sugar Amino Acids; 5.7 Cyclodextrin-Peptide Conjugates; 5.8 Carboproteins: Protein Models on Carbohydrate Templates; 5.9 Conclusion; References; 6 De Novo Design of Proteins; 6.1 Introduction 6.2 Secondary Structure Elements6.2.1 The -helix; 6.2.2 The -sheet; 6.2.3 Loops, Turns and Templates; 6.3 Assembling a Specified Tertiary Structure from Secondary Structural Elements; 6.3.1 Computational Methods; 6.3.2 Coiled Coils; 6.3.3 -helical Bundles; 6.3.4 Fluorous Interactions; 6.3.5 Additional Topics; 6.4 Proteins on Templates; 6.5 Foldamers; 6.6 Biopharmaceutical Applications of De Novo Design; 6.6.1 -helical Structures in Biopharmaceutical Applications; 6.6.2 Foldamers in Biopharmaceutical Applications; References 7 Design of Insulin Variants for Improved Treatment of Diabetes |
| Record Nr. | UNINA-9910139761503321 |
| West Sussex, UK ; ; Hoboken, NJ, : Wiley, 2009 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Pseudo-peptides in drug discovery [[electronic resource] /] / [edited by] Peter E. Neilsen
| Pseudo-peptides in drug discovery [[electronic resource] /] / [edited by] Peter E. Neilsen |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2004 |
| Descrizione fisica | 1 online resource (258 p.) |
| Disciplina | 615.19 |
| Altri autori (Persone) | NielsenPeter E. <1951-> |
| Soggetto topico |
Peptide drugs - Design
Peptides Amino acids - Synthesis Polyamides |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-280-52069-8
9786610520695 3-527-60569-X 3-527-60190-2 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Pseudo-peptides in Drug Discovery; Contents; Preface; List of Contributors; 1 Versatile Oligo(N-Substituted) Glycines: The Many Roles of Peptoids in Drug Discovery; 1.1 Introduction; 1.2 Peptoid Synthesis; 1.2.1 Solid-Phase Synthesis; 1.2.2 Sub-monomer Solid-Phase Method; 1.2.3 Side Reactions; 1.2.4 Post-Synthetic Analysis; 1.3 Drug Discovery via Small-Molecule Peptoid Libraries; 1.3.1 Peptoid Drugs from Combinatorial Libraries; 1.3.2 Peptoid Inhibitors of RNA-Protein Interactions; 1.4 Peptoid-Based Drug Delivery and Molecular Transporters: Cellular Uptake
1.4.1 Peptoid Mimics of HIV-Tat Protein1.4.2 Cellular Delivery of Nucleic Acids; 1.5 Peptoid Mimics of Peptide Ligands; 1.6 Peptoids with Folded Structure; 1.6.1 Restricting Conformational Space; 1.6.2 Peptoid Helices; 1.6.2.1 CD and NMR Studies of a Helical Peptoid Pentamer with α-Chiral Aromatic Side Chains; 1.6.2.2 CD Studies of Longer Peptoid Helices Containing α-Chiral Aromatic Side Chains; 1.6.2.3 Structural Studies of Peptoids with Aliphatic Side Chains by CD, NMR, and X-ray Crystallography; 1.6.2.4 Summary; 1.6.3 Protein-mimetic Structures 1.7 Biomimetic Peptoid Structures for Therapeutic Applications1.7.1 Peptoid Mimics of Antibacterial Peptides; 1.7.2 Peptoid-Based Mimics of Lung Surfactant Proteins; 1.7.3 Collagen-based Structures Containing Peptoid Residues; 1.8 Obstacles to the Development of Biomedically-useful Peptoids; 1.8.1 Enhance the Diversity of Secondary Structure in Peptoid Foldamers; 1.8.2 Improve Understanding of Peptoid Sequence/Structure Relationships; 1.8.3 Translate Bioactive Peptide Sequences into Bioactive Peptoid Sequences; 1.8.4 Develop Peptoids with Stable Tertiary Structure 1.8.5 Develop Peptoid Shuttles for Intracellular Import of Xenobiotic Agents1.8.6 Optimize Pharmacological Profile of Oligopeptoids; 1.9 Conclusion; 1.10 References; 2 β-Peptides, γ-Peptides and Isosteric Backbones: New Scaffolds with Controlled Shapes for Mimicking Protein Secondary Structure Elements; 2.1 Introduction; 2.2 Molecular Organization in β-Peptide Oligomers; 2.2.1 Historical Background; 2.2.2 β-Amino Acids versus α-Amino Acids: An Enormous Increase in Chemical Diversity; 2.2.3 Helical Folds; 2.2.3.1 The 3(14)-Helix; 2.2.3.2 The 12/10- (10/12-) Helix; 2.2.3.3 The 2.5(12)-Helix 2.2.3.4 The 2(8)-Helix2.2.4 Extended β-Peptide Strands, Turns and Formation of Sheet Structures; 2.3 Molecular Organization in γ-Peptide Oligomers; 2.3.1 Preparation of γ-Amino Acid Monomers for γ-Peptide Synthesis; 2.3.2 Helical Folds; 2.3.3 Turn and Sheet Structures; 2.4 Biological Activities of β- and γ-Peptides; 2.4.1 Biological Stability; 2.4.2 Bioactive Peptides Based on Helical Scaffolds; 2.4.3 Bioactive Peptides Based on Open-Chain β-Turn Mimetics; 2.4.4 Cell Penetrating β-Peptides; 2.5 Isosteres; 2.5.1 Example 1: Oligomers of α-Aminooxy Acids as β-Peptide Mimetics 2.5.2 Example 2: N,N ́-Linked Oligoureas as γ-Peptide Mimetics |
| Record Nr. | UNINA-9910146238203321 |
| Weinheim, : Wiley-VCH, c2004 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Pseudo-peptides in drug discovery [[electronic resource] /] / [edited by] Peter E. Neilsen
| Pseudo-peptides in drug discovery [[electronic resource] /] / [edited by] Peter E. Neilsen |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2004 |
| Descrizione fisica | 1 online resource (258 p.) |
| Disciplina | 615.19 |
| Altri autori (Persone) | NielsenPeter E. <1951-> |
| Soggetto topico |
Peptide drugs - Design
Peptides Amino acids - Synthesis Polyamides |
| ISBN |
1-280-52069-8
9786610520695 3-527-60569-X 3-527-60190-2 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Pseudo-peptides in Drug Discovery; Contents; Preface; List of Contributors; 1 Versatile Oligo(N-Substituted) Glycines: The Many Roles of Peptoids in Drug Discovery; 1.1 Introduction; 1.2 Peptoid Synthesis; 1.2.1 Solid-Phase Synthesis; 1.2.2 Sub-monomer Solid-Phase Method; 1.2.3 Side Reactions; 1.2.4 Post-Synthetic Analysis; 1.3 Drug Discovery via Small-Molecule Peptoid Libraries; 1.3.1 Peptoid Drugs from Combinatorial Libraries; 1.3.2 Peptoid Inhibitors of RNA-Protein Interactions; 1.4 Peptoid-Based Drug Delivery and Molecular Transporters: Cellular Uptake
1.4.1 Peptoid Mimics of HIV-Tat Protein1.4.2 Cellular Delivery of Nucleic Acids; 1.5 Peptoid Mimics of Peptide Ligands; 1.6 Peptoids with Folded Structure; 1.6.1 Restricting Conformational Space; 1.6.2 Peptoid Helices; 1.6.2.1 CD and NMR Studies of a Helical Peptoid Pentamer with α-Chiral Aromatic Side Chains; 1.6.2.2 CD Studies of Longer Peptoid Helices Containing α-Chiral Aromatic Side Chains; 1.6.2.3 Structural Studies of Peptoids with Aliphatic Side Chains by CD, NMR, and X-ray Crystallography; 1.6.2.4 Summary; 1.6.3 Protein-mimetic Structures 1.7 Biomimetic Peptoid Structures for Therapeutic Applications1.7.1 Peptoid Mimics of Antibacterial Peptides; 1.7.2 Peptoid-Based Mimics of Lung Surfactant Proteins; 1.7.3 Collagen-based Structures Containing Peptoid Residues; 1.8 Obstacles to the Development of Biomedically-useful Peptoids; 1.8.1 Enhance the Diversity of Secondary Structure in Peptoid Foldamers; 1.8.2 Improve Understanding of Peptoid Sequence/Structure Relationships; 1.8.3 Translate Bioactive Peptide Sequences into Bioactive Peptoid Sequences; 1.8.4 Develop Peptoids with Stable Tertiary Structure 1.8.5 Develop Peptoid Shuttles for Intracellular Import of Xenobiotic Agents1.8.6 Optimize Pharmacological Profile of Oligopeptoids; 1.9 Conclusion; 1.10 References; 2 β-Peptides, γ-Peptides and Isosteric Backbones: New Scaffolds with Controlled Shapes for Mimicking Protein Secondary Structure Elements; 2.1 Introduction; 2.2 Molecular Organization in β-Peptide Oligomers; 2.2.1 Historical Background; 2.2.2 β-Amino Acids versus α-Amino Acids: An Enormous Increase in Chemical Diversity; 2.2.3 Helical Folds; 2.2.3.1 The 3(14)-Helix; 2.2.3.2 The 12/10- (10/12-) Helix; 2.2.3.3 The 2.5(12)-Helix 2.2.3.4 The 2(8)-Helix2.2.4 Extended β-Peptide Strands, Turns and Formation of Sheet Structures; 2.3 Molecular Organization in γ-Peptide Oligomers; 2.3.1 Preparation of γ-Amino Acid Monomers for γ-Peptide Synthesis; 2.3.2 Helical Folds; 2.3.3 Turn and Sheet Structures; 2.4 Biological Activities of β- and γ-Peptides; 2.4.1 Biological Stability; 2.4.2 Bioactive Peptides Based on Helical Scaffolds; 2.4.3 Bioactive Peptides Based on Open-Chain β-Turn Mimetics; 2.4.4 Cell Penetrating β-Peptides; 2.5 Isosteres; 2.5.1 Example 1: Oligomers of α-Aminooxy Acids as β-Peptide Mimetics 2.5.2 Example 2: N,N ́-Linked Oligoureas as γ-Peptide Mimetics |
| Record Nr. | UNISA-996204197303316 |
| Weinheim, : Wiley-VCH, c2004 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. di Salerno | ||
| ||
Pseudo-peptides in drug discovery [[electronic resource] /] / [edited by] Peter E. Neilsen
| Pseudo-peptides in drug discovery [[electronic resource] /] / [edited by] Peter E. Neilsen |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2004 |
| Descrizione fisica | 1 online resource (258 p.) |
| Disciplina | 615.19 |
| Altri autori (Persone) | NielsenPeter E. <1951-> |
| Soggetto topico |
Peptide drugs - Design
Peptides Amino acids - Synthesis Polyamides |
| ISBN |
1-280-52069-8
9786610520695 3-527-60569-X 3-527-60190-2 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Pseudo-peptides in Drug Discovery; Contents; Preface; List of Contributors; 1 Versatile Oligo(N-Substituted) Glycines: The Many Roles of Peptoids in Drug Discovery; 1.1 Introduction; 1.2 Peptoid Synthesis; 1.2.1 Solid-Phase Synthesis; 1.2.2 Sub-monomer Solid-Phase Method; 1.2.3 Side Reactions; 1.2.4 Post-Synthetic Analysis; 1.3 Drug Discovery via Small-Molecule Peptoid Libraries; 1.3.1 Peptoid Drugs from Combinatorial Libraries; 1.3.2 Peptoid Inhibitors of RNA-Protein Interactions; 1.4 Peptoid-Based Drug Delivery and Molecular Transporters: Cellular Uptake
1.4.1 Peptoid Mimics of HIV-Tat Protein1.4.2 Cellular Delivery of Nucleic Acids; 1.5 Peptoid Mimics of Peptide Ligands; 1.6 Peptoids with Folded Structure; 1.6.1 Restricting Conformational Space; 1.6.2 Peptoid Helices; 1.6.2.1 CD and NMR Studies of a Helical Peptoid Pentamer with α-Chiral Aromatic Side Chains; 1.6.2.2 CD Studies of Longer Peptoid Helices Containing α-Chiral Aromatic Side Chains; 1.6.2.3 Structural Studies of Peptoids with Aliphatic Side Chains by CD, NMR, and X-ray Crystallography; 1.6.2.4 Summary; 1.6.3 Protein-mimetic Structures 1.7 Biomimetic Peptoid Structures for Therapeutic Applications1.7.1 Peptoid Mimics of Antibacterial Peptides; 1.7.2 Peptoid-Based Mimics of Lung Surfactant Proteins; 1.7.3 Collagen-based Structures Containing Peptoid Residues; 1.8 Obstacles to the Development of Biomedically-useful Peptoids; 1.8.1 Enhance the Diversity of Secondary Structure in Peptoid Foldamers; 1.8.2 Improve Understanding of Peptoid Sequence/Structure Relationships; 1.8.3 Translate Bioactive Peptide Sequences into Bioactive Peptoid Sequences; 1.8.4 Develop Peptoids with Stable Tertiary Structure 1.8.5 Develop Peptoid Shuttles for Intracellular Import of Xenobiotic Agents1.8.6 Optimize Pharmacological Profile of Oligopeptoids; 1.9 Conclusion; 1.10 References; 2 β-Peptides, γ-Peptides and Isosteric Backbones: New Scaffolds with Controlled Shapes for Mimicking Protein Secondary Structure Elements; 2.1 Introduction; 2.2 Molecular Organization in β-Peptide Oligomers; 2.2.1 Historical Background; 2.2.2 β-Amino Acids versus α-Amino Acids: An Enormous Increase in Chemical Diversity; 2.2.3 Helical Folds; 2.2.3.1 The 3(14)-Helix; 2.2.3.2 The 12/10- (10/12-) Helix; 2.2.3.3 The 2.5(12)-Helix 2.2.3.4 The 2(8)-Helix2.2.4 Extended β-Peptide Strands, Turns and Formation of Sheet Structures; 2.3 Molecular Organization in γ-Peptide Oligomers; 2.3.1 Preparation of γ-Amino Acid Monomers for γ-Peptide Synthesis; 2.3.2 Helical Folds; 2.3.3 Turn and Sheet Structures; 2.4 Biological Activities of β- and γ-Peptides; 2.4.1 Biological Stability; 2.4.2 Bioactive Peptides Based on Helical Scaffolds; 2.4.3 Bioactive Peptides Based on Open-Chain β-Turn Mimetics; 2.4.4 Cell Penetrating β-Peptides; 2.5 Isosteres; 2.5.1 Example 1: Oligomers of α-Aminooxy Acids as β-Peptide Mimetics 2.5.2 Example 2: N,N ́-Linked Oligoureas as γ-Peptide Mimetics |
| Record Nr. | UNINA-9910830060603321 |
| Weinheim, : Wiley-VCH, c2004 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Pseudo-peptides in drug discovery / / [edited by] Peter E. Neilsen
| Pseudo-peptides in drug discovery / / [edited by] Peter E. Neilsen |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2004 |
| Descrizione fisica | 1 online resource (258 p.) |
| Disciplina | 615.19 |
| Altri autori (Persone) | NielsenPeter E. <1951-> |
| Soggetto topico |
Peptide drugs - Design
Peptides Amino acids - Synthesis Polyamides |
| ISBN |
1-280-52069-8
9786610520695 3-527-60569-X 3-527-60190-2 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Pseudo-peptides in Drug Discovery; Contents; Preface; List of Contributors; 1 Versatile Oligo(N-Substituted) Glycines: The Many Roles of Peptoids in Drug Discovery; 1.1 Introduction; 1.2 Peptoid Synthesis; 1.2.1 Solid-Phase Synthesis; 1.2.2 Sub-monomer Solid-Phase Method; 1.2.3 Side Reactions; 1.2.4 Post-Synthetic Analysis; 1.3 Drug Discovery via Small-Molecule Peptoid Libraries; 1.3.1 Peptoid Drugs from Combinatorial Libraries; 1.3.2 Peptoid Inhibitors of RNA-Protein Interactions; 1.4 Peptoid-Based Drug Delivery and Molecular Transporters: Cellular Uptake
1.4.1 Peptoid Mimics of HIV-Tat Protein1.4.2 Cellular Delivery of Nucleic Acids; 1.5 Peptoid Mimics of Peptide Ligands; 1.6 Peptoids with Folded Structure; 1.6.1 Restricting Conformational Space; 1.6.2 Peptoid Helices; 1.6.2.1 CD and NMR Studies of a Helical Peptoid Pentamer with α-Chiral Aromatic Side Chains; 1.6.2.2 CD Studies of Longer Peptoid Helices Containing α-Chiral Aromatic Side Chains; 1.6.2.3 Structural Studies of Peptoids with Aliphatic Side Chains by CD, NMR, and X-ray Crystallography; 1.6.2.4 Summary; 1.6.3 Protein-mimetic Structures 1.7 Biomimetic Peptoid Structures for Therapeutic Applications1.7.1 Peptoid Mimics of Antibacterial Peptides; 1.7.2 Peptoid-Based Mimics of Lung Surfactant Proteins; 1.7.3 Collagen-based Structures Containing Peptoid Residues; 1.8 Obstacles to the Development of Biomedically-useful Peptoids; 1.8.1 Enhance the Diversity of Secondary Structure in Peptoid Foldamers; 1.8.2 Improve Understanding of Peptoid Sequence/Structure Relationships; 1.8.3 Translate Bioactive Peptide Sequences into Bioactive Peptoid Sequences; 1.8.4 Develop Peptoids with Stable Tertiary Structure 1.8.5 Develop Peptoid Shuttles for Intracellular Import of Xenobiotic Agents1.8.6 Optimize Pharmacological Profile of Oligopeptoids; 1.9 Conclusion; 1.10 References; 2 β-Peptides, γ-Peptides and Isosteric Backbones: New Scaffolds with Controlled Shapes for Mimicking Protein Secondary Structure Elements; 2.1 Introduction; 2.2 Molecular Organization in β-Peptide Oligomers; 2.2.1 Historical Background; 2.2.2 β-Amino Acids versus α-Amino Acids: An Enormous Increase in Chemical Diversity; 2.2.3 Helical Folds; 2.2.3.1 The 3(14)-Helix; 2.2.3.2 The 12/10- (10/12-) Helix; 2.2.3.3 The 2.5(12)-Helix 2.2.3.4 The 2(8)-Helix2.2.4 Extended β-Peptide Strands, Turns and Formation of Sheet Structures; 2.3 Molecular Organization in γ-Peptide Oligomers; 2.3.1 Preparation of γ-Amino Acid Monomers for γ-Peptide Synthesis; 2.3.2 Helical Folds; 2.3.3 Turn and Sheet Structures; 2.4 Biological Activities of β- and γ-Peptides; 2.4.1 Biological Stability; 2.4.2 Bioactive Peptides Based on Helical Scaffolds; 2.4.3 Bioactive Peptides Based on Open-Chain β-Turn Mimetics; 2.4.4 Cell Penetrating β-Peptides; 2.5 Isosteres; 2.5.1 Example 1: Oligomers of α-Aminooxy Acids as β-Peptide Mimetics 2.5.2 Example 2: N,N ́-Linked Oligoureas as γ-Peptide Mimetics |
| Record Nr. | UNINA-9910877163103321 |
| Weinheim, : Wiley-VCH, c2004 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Soggetto topico
-
Peptide drugs - Design
(5)
- Amino acids - Synthesis (4)
- Peptides (4)
- Polyamides (4)
- Peptides - Design (1)