Part One. Synthesis and Chemistry of Modified Amino Acids.

1. Synthesis and Chemistry of α,ß-Didehydroamino Acids (Uli Kazmaier).

1.1 Introduction.

1.2 Synthesis of DDAAs.

1.3 Reactions of DDAAs.

1.4 Conclusions.

1.5 Experimental Procedures.

References.

2. Synthesis and Chemistry of α-Hydrazino Acids (Joëlle Vidal).

2.1 Indroduction.

2.2 Synthesis.

2.3 Chemistry.

2.4 Conclusions.

2.5 Experimental Procedures.

References.

3. Hydroxamic Acids: Chemistry, Bioactivity, and Solution-and Solid-Phase Synthesis (Darren Griffith, Marc Devocelle, and Celine J. Marmion).

3.1 Introduction.

3.2 Chemistry, Bioactivity, and Clinical Utility.

3.3 Solution-Phase Synthesis of Hydroxamic Acids.

3.4 Solid-Phase Synthesis of Hydroxamic Acids.

3.5 Conclusions.

3.6 Experimental Procedures.

References.

4. Chemistry of α-Aminoboronic Acids and their Deriatives (Valery M. Dembitsky and Morris Srebnick).

4.1 Introduction.

4.2 Synthesis of α-Aminoboronic Acids.

4.3 Synthesis of α-Aminoboronic Acid Derivatives.

4.4 Asymmetric of Synthesis via α-Haloalkylboronic Esters.

4.5 Synthesis of Glycine α-Aminoboronic Acids.

4.6 Synthesis of Proline α-Aminoboronic Acids.

4.7 Synthesis of Alanine α-Aminoboronic Acids.

4.8 Synthesis of Ornithine α-Aminoboronic Acids.

4.9 Synthesis of Arginine α-Aminoboronic Acids.

4.10 Synthesis of Phenethyl Peptide Boronic Acids.

4.11 Synthesis via Zirconocene Species.

4.12 Synthesis and Activity of Amine-Carboxyboranes and their Derivations,

4.13 Synthesis of Boron Analogs of Phosphonoacetates.

4.14 Conclusions.

References.

5. Chemistry of Aminophosphonic Acids and Phosphonopeptides (Valery P. Kukhar and Vadim D. Romanenko).

5.1 Introduction.

5.2 Physical/Chemical Properties and Analysis.

5.3 Synthesis of α-Aminophosphonic Acids.

5.4 Synthesis of ß-Aminophosphonates.

5.5 Synthesis of γ-Aminophosphonates and Higher Homologs.

5.6 Phosphono- and Phosphinopeptides.

5.7 Remarks on the Practical Utility of Aminophosphonates.

5.8 Conclusions.

5.9 Experimental Procedures.

References.

6. Chemistry of Silicon-Containing Amino Acids (Yingmei Qi and Scott McN. Sieburth).

6.1 Introduction.

6.2 Synthesis of Silicon-Containing Amino Acids.

6.3 Reactions of Silicon-Containing Amino Acids.

6.4 Bioactive Peptides Incorporating Silicon-Substituted Amino Acids.

6.5 Conclusions.

References.

Part Two. Amino Acid Organocatalysis.

7. Catalysis of Reactions by Amino Acids (Haibo Xie, Thomas Hayes, and Nicholas Gathergood).

7.1 Introduction.

7.2 Aldol Reaction.

7.3 Mannich Reaction.

7.4 α-Amination Reaction.

7.5 Michael Reaction.

7.6 Morita-Baylis-Hillman Reaction and Its Aza-Counterpart.

7.7 Miscellaneous Amino Acid-Catalyzed Reactions.

7.8 Sustainability of Amino Acid Catalysis.

7.9 Conclusions and Expectations.

7.10 Typical Procedures for Preferred Catalysis of Reactions by Amino Acids.

References.

Part Three. Enzymes.

8. Proteases as Powerful Catalysts for Organic Synthesis (Andrés Illanes, Fanny Guzmán, and Sonia Barberis).

8.1 Enzyme Biocatalysis.

8.2 Proteolytic Enzymes: Mechanisms and Characteristics.

8.3 Proteases as Process Catalysts.

8.4 Proteases in Organic Synthesis.

8.5 Peptide Synthesis.

8.6 Conclusions.

References.

9. Semisynthetic Enzymes (Usama M. Hegazy and Bengt Mannevik).

9.1 Usefulness of Semisynthetic Enzymes.

9.2 Natural Protein Biosynthesis.

9.3 Sense Codon Reassignment.

9.4 Missense Suppression.

9.5 Evolving the Orthogonal aaRS/tRNA Pair.

9.6 Nonsense Suppression.

9.7 Mischarging of tRNA by Ribozyme.

9.8 Evolving the Orthogonal Ribosome/mRNA Pair.

9.9 Frame-Shift Suppression.

9.10 Noncanonical Base Pairs.

9.11 Chemical Ligation.

9.12 Inteins.

9.13 EPL.

9.14 Post-Translational Chemical Modification.

9.15 Examples of Semisynthetic Enzymes.

9.16 Conclusions.

References.

10. Catalysis by Peptide-Based Enzyme Models (Giovanna Ghirlanda, Leonard J. Prins, and Paolo Scimin).

10.1 Introduction.

10.2 Peptide Models of Hydrolytic Enzymes.

10.3 Peptide Models of Heme Proteins.

  10.4 Conclusions.

References.

11. Substate Recognition (Keith Brocklehurst, Sheraz Gul, and Richard W. Pickersgill).

11.1 Recognition, Specificity, Catalysis, Inhibition, and Linguistics.

11.2 Serine Proteinases.

11.3 Cysteine Proteinases.

11.4 Glycoside Hydrolases.

11.5 Protein Kinases.

11.6 aaRSs.

11.7 Lipases.

11.8 Conclusions.

References.

12. Protein Recognition (Robyn E. Mansfield, Arwen J. Cross, Jacqueline M. Matthews, and Joel P. Mackay).

12.1 General Introduction.

12.2 Nature of Protein Interfaces.

12.3 Affinity of Protein Interactions.

12.4 Measuring Protein Interactions.

12.5 Coupled Folding and Binding.

12.6 Regulation of Interactions by PTMs.

12.7 Engineering and Inhibiting Protein-Protein Interactions.

12.8 Conclusions.

References.

13. Mammalian Peptide Hormones: Biosynthesis and Inhibition (Karen Brand and Annette G. Beck-Sickinger).

13.1 Introduction.

13.2 Mammalian Peptide Hormones.

13.3 Biosynthesis of Peptide Hormones.

13.4 Inhibition of Biosynthesis.

13.5 Conclusions.

References.

14. Insect Peptide Hormones (R. Elwyn Isaac and Neil Audsley).

14.1 Introduction.

14.2 Structure and Biosynthesis of Insect Peptide Hormones.

14.3 Proctolin.

14.4 Sex Peptide.

14.5 A-Type Allatostatins.

14.6 CRF-Related Diuretic Hormones (DH).

14.7 Insect Peptide Hormones and Insect Control.

14.8 Conclusions.

References.

15. Plant Peptide Signals (Javier Narváez-Vásquez, Martha L. Orozco-Cárdenas, and Gregory Pearce).

15.1 Introduction.

15.2 Defense-Related Peptides.

15.3 Peptides Involved in Growth and Development.

15.4 Peptides Involved in Self-Recognition.

15.5 Methods in Plant Regulatory Peptide Research.

15.6 Conclusions.

References.

16. Nonribosomal Peptide Synthesis (Sean Doyle).

16.1 Introduction.

16.2 NRPs.

16.3 NRP Synthetase Domains.

16.4 PPTases.

16.5 Experimental Strategies for NRPS Investigations.

16.6 Non-NRPS.

16.7 Conclusions.

References.

Index.