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Characterization of polyamide 66 obturator materials by differential scanning calorimetry and size-exclusion chromatography [[electronic resource] /] / Frederick L. Beyer, Eugene Napadensky, Christopher R. Ziegler
| Characterization of polyamide 66 obturator materials by differential scanning calorimetry and size-exclusion chromatography [[electronic resource] /] / Frederick L. Beyer, Eugene Napadensky, Christopher R. Ziegler |
| Autore | Beyer Frederick L |
| Pubbl/distr/stampa | Aberdeen Proving Ground, MD : , : Army Research Laboratory, , [2005] |
| Descrizione fisica | 1 online resource (vi, 16 pages) : illustrations |
| Altri autori (Persone) |
NapadenskyEugene
ZieglerChristopher R |
| Collana | ARL-TR |
| Soggetto topico |
Polyamides
Chromatographic analysis |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Altri titoli varianti | Characterization of polyamide sixty six obturator materials by differential scanning calorimetry and size exclusion chromatography |
| Record Nr. | UNINA-9910697042103321 |
Beyer Frederick L
|
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| Aberdeen Proving Ground, MD : , : Army Research Laboratory, , [2005] | ||
| 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 | ||
| ||
