Preface
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Published:12 Nov 2013
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E. Farkas and M. Ryadnov, in Amino Acids, Peptides and Proteins, ed. E. Farkas and M. Ryadnov, The Royal Society of Chemistry, 2013, vol. 38, pp. P005-P006.
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This volume continues the legacy of the annual report series launched in 1969 and re-launched last year after a five-year break. The main objective of the series has been to provide a comprehensive review coverage of research progress, both critical and systematic, in peptide and protein science. Each volume of the series strives to highlight the most recent findings and developments in specific research areas and reviewes literature predominantly published over the last two-three years. Routine revisions of more traditional concepts in the light of emerging discoveries, and vice versa, constitute an integral part of each chapter, which makes this series unique and different from other publications and allows keeping pace with the progress without losing touch with foundations.
The volume starts with an overview of oxidative transformations catalysed by a prominent class of oxidoreductases, cytochromes P450 (Cryle, Brieke and Haslinger). This chapter builds around the mechanistic, reactive and structural aspects of cytochrome-mediated oxidation of amino acids and peptides with functional implications for primary and secondary metabolism including the biosynthesis of important depsi- and glycopeptide toxins and antibiotics. A stronger focus on the high-resolution structural elucidation of peptide macrocylisation through cystine formation is made in the following chapter (Kövér and Batta) which gives an overview of NMR investigations of complex cystine-knot structures of plant antibiotics, cyclotides, and cystine ladder motifs of antimicrobial θ-defensins, also covering ion channel blockers and other small cysteine-rich proteins. This chapter is followed by an overview of one of the most biomedically prominent peptide families – relaxin family peptide hormones (Chan, Samuel, Separovic, Hossain and Wade). A specific emphasis is made here on the unique cystine-knot-like structural properties of the peptides that determine their role in fibrotic diseases. The biological function of peptide sequences is reviewed from the perspective of de novo peptide design highlighting pros and cons of autonomously folded and self-assembling backbone motifs (Ryadnov), with the following chapter giving a detailed overview of nanomaterial applications of peptide self-assembly ranging from electronic devices to self-assembly-templated mineralization (Tsutsumi and Mihara). Emerging high-resolution technologies for the characterisation of peptide and protein structures in native dynamic environments, such as protein folds and peptidomes, are reviewed in two subsequent chapters, first, outlining the applicability of peptide distance constraints derived from mass spectrometry analyses of chemically cross-linked peptides for protein structure elucidation (Henrion), and, second, giving an overview of recent developments in peptidome analysis and biomarker discovery, involving endogenous and exogenous peptides, in the context of mainstream analytical tools and technologies (Rakowska and Ryadnov). The volume closes with a comprehensive coverage of marketed peptide and protein pharmaceuticals and progress in the development of emerging peptide-based drugs (Mezó). Each chapter is structured around current trends in the reviewed research area that are compared with more established approaches wherever possible, and the authors' outlook of future perspectives, either as a separate section or incorporated in the text. All chapters are written by leading researchers in their subject areas to enable a worldwide information source of broad appeal to researchers in academia and industry.