Peptide Chemistry: A Practical Textbook (1988)

I. Introduction.- References and Additional Sources.- One: Structure Determination.- II. Amino Acid Analysis.- Additonal Sources.- III. Sequence Determination.- A. End Group Determination.- 1. Determination of the N-terminal Residue.- 2. Determination of the C-terminal Residue.- B. Sequential Degradation.- 1. Hydrolysis Catalyzed by Exopeptidases.- 2. Edman Degradation.- a) The Two-step Procedure.- b) The Three-step Procedure.- c) Automated Sequencing.- d) The Edman-Dansyl Process.- C. Sequence Determination with the Help of Mass Spectra.- D. Fragmentation of Peptides.- 1. Hydrolysis with Specific Endopeptidases.- 2. Chemical Methods of Cleavage.- 3. Fission of Disulfides.- References and Additional Sources.- IV. Secondary and Tertiary Structure.- A. Architectural Features Peptides.- 1. The Peptide Bond.- 2. Secondary Structures.- 3. Tertiary Structure.- 4. Quaternary Structure.- B. Methods for the Analysis of Conformation of Peptides.- 1. Optical Rotatory Dispersion and Circular Dichroism.- 2. Nuclear Magnetic Resonance (nmr) Spectroscopy.- 3. X-Ray Crystallography.- C. Prediction of Conformation Peptides.- References and Additional Sources.- Two: Peptide Synthesis.- V. Formation of the Peptide Bond.- A. The Acid Chloride Method.- B. The Acid Azide Method.- C. Anhydrides.- D. Active Esters.- E. Coupling Reagents.- F. Enzyme-catalyzed Bond Formation.- G. Non-conventional Methods of Peptide Bond Formation.- References.- Additional Sources.- VI. Protection of Functional Groups.- A. Blocking of ?-Amino Groups.- B. Blocking of Side Chain Amino Groups.- C. Protection of the Carboxyl Group.- D. Protection of Hydroxyl Groups.- E. Blocking of the Sulfhydryl Group.- F. Masking the Thioether Methionine.- G. Protection of the Guanidine Function the Arginine Side Chain.- H. Masking the Imidazole Histidine.- I. Indole Protection.- J. Carboxamide Blocking Groups.- References and Additional Sources.- VII. Undesired Reactions During Synthesis.- A. Base-catalyzed Ring Closure.- B. Acid-catalyzed Ring Closure.- C. Acyl Migration.- D. Alkylation.- E. Friedel-Crafts Reaction.- F. Saturation of Aromatic Nuclei.- G. Reductive Cleavage of the Peptide Chain.- H. Oxidative Decomposition of the Indole Tryptophan.- I. Side Reactions Caused by Steric Hindrance.- J. Prevention and Suppression of Side Reactions.- Additional Source.- VIII. Racemization.- A. Mechanism of Racemization.- B. Detection of Racemization.- C. Racemization Studies Model Systems.- D. Prevention of Racemization.- References and Additional Source.- IX. Design of Schemes for Peptide Synthesis.- A. Segment Condensation.- B. Stepwise Chain-lengthening Starting with the N-Terminal Residue.- C. Stepwise Chain-lengthening Starting with the C-Terminal Residue.- D. Tactical Considerations.- E. Synthesis of Special Target Peptides.- 1. Polyamino Acids and Sequential Polypeptides.- 2. Disulfide Bridges.- 3. Cyclic Peptides.- 4. Peptides Containing Non-amino Acid Constituents.- 5. Semisynthesis (Partial Synthesis).- References.- Additional Sources.- X. Solid Phase Peptide Synthesis.- A. The Insoluble Polymeric Support and the Bond Linking the Peptide to the Resin.- B. Removal of Temporary Blocking Groups.- C. Coupling: Acylation of the Resin-bound Amine-component.- D. Separation of the Completed Peptide Chain from the Polymeric Support and Final Deprotection.- E. Some Problems Encountered Solid Phase Peptide Synthesis.- 1. Premature Chain-termination.- 2. Deletion.- References and Additional Sources.- XI. Methods of Facilitation.- A. Chains Attached to a Soluble Polymer (The Liquid Phase Method).- B. The Picolyl Ester Method.- C. Rapid Synthesis.- 1. Chain-building Without Isolation of Intermediates.- 2. Chain-building Through Isolated Intermediates.- D. Synthesis in situ.- E. Simultaneous Synthesis of Peptide Analogs.- F. Insoluble Reagents.- 1. Active Esters.- 2. Polymeric Coupling Reagents.- 3. Insoluble Cleaving Reagents.- References and Additional Sources.- XII. Analysis and Characterization of Synthetic Peptides.- A. Homogeneity Tests.- B. Amino Acid Analysis and Sequence Determination.- C. Elemental Analysis.- D. Measurement of Optical Activity.- E. Infrared and Ultraviolet Absorption Spectra.- F. Nuclear Magnetic Resonance Spectra.- G. Molecular-weight Determination.- Reference and Additional Sources.