The architectures (three-dimensional shapes) of peptides determine their respective biological functions. Therefore, the correct alignment of functionalities in a structure by constraining the flexibility is a key process in evolution as well as in medicinal chemistry in order to increase binding affinity and selectivity. The rigidification of a peptide chain can have local effects (incorporation of the amino acid proline) or it can globally restrain flexibility (macrocyclization). Furthermore, the combination of both strategies has given rise to complex antibiotics with highly optimized modes of action. This work approaches these principles in three topics and for different purposes. The first chapter presents a novel scanning strategy which utilizes synthetic local rigidifications for the evaluation of Neuropeptide Y structure and receptor binding patterns. The fundamental process of macrocyclization is topic of the second chapter. For iminopeptides, ring-chain equilibria can be established and controlled, thereby allowing for the thermodynamic analysis of the ring closure. This leads to the identification of structural determinants that influence the inclination of a peptide chain to close the ring. In the third chapter, a sugarbased synthetic pathway leading to highly functionalized thiazole dipeptides is described. This strategy led to the synthesis of core motivs of complex thiopeptide antibiotics, as well as to diastereomers and homologs thereof.

Organic chemists working on the synthesis of natural products have long found a special challenge in the preparation of peptides and proteins. However, more reliable, more efficient synthetic preparation methods have been developed in recent years. This reference evaluates the most important synthesis methods available today, and also considers methods that show promise for future applications. This text describes the state of the art in efficient synthetic methods for the synthesis of both natural and artificial large peptide and protein molecules. Subjects include an introduction to basic topics, linear solid-phase synthesis of peptides, peptide synthesis in solution, convergent solid-phase synthesis, methods for the synthesis of branched peptides, formation of disulfide bridges, and more. The book emphasizes strategies and tactics that must be considered for the successful synthesis of peptides.

The Peptides: Analysis, Synthesis, Biology: Volume 4: Modern Techniques of Conformational, Structural, and Configurational Analysis is an open-ended treatise that provides comprehensive and critical reviews of important developments in all areas of peptide research including analysis, synthesis, and biology. X-ray structure studies, amino acid analysis, and chiroptical analysis of configuration are discussed, along with solid-phase sequencing and ultramicroanalysis with the aid of fluorescence. This volume is comprised of six chapters and begins with an account of crystal structure analysis on molecules containing 2-12 peptide units, focusing on the variety of intramolecular hydrogen bonds, cis peptide units, and multiple conformation. Conformational changes upon complexation with metal ions are considered, together with the inclusion of solvents as integral parts of a molecular structure. The following chapters explore the conformations of insulin, glucagon, pancreatic polypeptide and related molecules, as well as the molecular biology of these hormones based on crystal structures; the usefulness of chiroptical techniques for determining the absolute configuration of amino acids and small peptides; and ultramicroanalysis of peptides and proteins by high performance liquid chromatography and fluorescence detection. The final chapter looks at the status and future potential of solid-phase sequencing. This book is intended as a reference for specialists, a guide for the novice, and a forum for investigators concerned with research on peptides and proteins.

Doctoral Thesis / Dissertation from the year 2004 in the subject Chemistry - Organic Chemistry, Bangalore University / Central College (Department of Studies in Chemistry), language: English, abstract: The importance of ß-amino acids has been focused, particularly in the past few decades. They are found as components of many biologically active peptidic and nonpeptidic natural products with antibiotic, antifungal, cytotoxic, and other pharmacological properties. ß-Amino acids are produced in humans, animals, microorganisms, marine organisms, and plants either in free state or as part of a peptide or depsipeptide. The importance of nonpeptidic ß-amino acids has been nfocused particularly on the ß-lactam antibiotics, since naturally occurring penicillin derivatives have been discovered as broad antibiotic active agents. Over the years, a large number of these compounds have been prepared and tested, and a variety of new ß-lactam ring systems have been introduced such as cephems, cephalosporins, oxacephems, penems, carbapenems, oxapenams as well as monocyclic and polycyclic ring systems. ß-Amino acids have been known to play an important role in primary and secondary metabolism also. [...]

No detailed description available for "Principles of Peptide Synthesis".

The Peptides: Analysis, Synthesis, Biology, Volume 1: Major Methods of Peptide Bond Formation provides comprehensive and critical reviews of important developments in three major areas of peptide research—analysis, synthesis, and biology. This book discusses the nature of the peptide bond, coupling between amino acid residues, and catalysis of active ester reactions. The formation of hydrazides, reactions of carbodiimides with amines, and mixed carbonic anhydride method of peptide synthesis are also elaborated. This publication likewise covers the control of racemization during peptide synthesis, strategies for minimizing racemization during amide-forming steps, and assays for chiral purity. This volume is suitable for students, specialists, and scientists from a broad range of disciplines concerned with peptides.