Principles of Peptide Synthesis

I. Introduction.- References.- II. Activation and Coupling.- 1 Activation.- 2 Coupling.- 3 Coupling Methods.- References.- III. Reversible Blocking of Amino and Carboxyl Groups.- 1 General Aspects.- 2 Protection of the Carboxyl Group.- 3 Protection of the Amino Group.- References.- IV. Semipermanent Protection of Side Chain Functions.- 1 Carboxyl Groups of Aspartyl and Glutamyl Residues.- 2 Side Chain Amino Groups of Lysine and Ornithine.- 3 Hydroxyl Groups in Serine, Threonine and Tyrosine.- 4 The Sulfhydryl Group in Cysteine.- 5 The Guanidino Group of Arginine.- 6 Imidazole in Histidine.- 7 The Thioether in Methionine.- 8 The Indole Nitrogen in Tryptophan.- 9 The Carboxamide Groups in Asparagine and Glutamine.- References.- V. Side Reactions in Peptide Synthesis.- 1 Side Reactions Initiated by Proton Abstraction.- 2 Side Reactions Initiated by Protonation.- 3 Side Reactions Due to Overactivation.- 4 Side Reactions Related to Individual Amino Acid Residues.- References.- VI. Tactics and Strategy in Peptide Synthesis.- 1 Tactics.- 2 Strategies.- 3 Disulfide Bridges.- 4 Synthesis of Cyclic Peptides.- 5 Sequential Polypeptides.- 6 Partial Synthesis (Semisynthesis).- References.- VII. Techniques for the Facilitation of Peptide Synthesis.- 1 Solid Phase Peptide Synthesis (SPPS).- 2 Synthesis in Solution.- References.- VIII Recent Developments, New Trends.- 1 Formation of the Peptide Bond.- 2 Protecting Groups.- 3 Solid Phase Peptide Synthesis.- 4 Undesired Reactions in Peptide Synthesis.- 5 New Trends and Perspectives.- References.