Editorial

Abstract

The papers in this issue of Peptide Science reflect the scientific identity of the journal, as well as the truly international character of the field of peptide chemistry and biology. We are very pleased to present a review solicited from one of the recipients of the 2004 Vincent du Vigneaud Awards from the American Peptide Society. Dieter Seebach of the ETH, Zurich, was honored for “the discovery of peptides consisting of homologated proteinogenic amino acids and of their unexpected chemical, structural, and biological properties.” His review in this issue provides an extensive discussion of β-amino acids, specifically those with side chains in the carbonyl position, including their occurrence in nature, their synthesis, and their uses in design of novel peptide properties. We congratulate Dieter for this richly deserved recognition, and we thank him for providing an exciting review to Peptide Science. The original papers appearing in this issue epitomize the field of peptide science and illustrate the power of peptide synthesis and conformational study: Chakrabarty and coworkers present results of peptide design aimed at deducing the principles for helical bundle formation. Their work explores factors important in packing of α-helices and shows how peptide studies can shed light on fundamental ‘rules’ for the formation of protein architectures. The use of synthetic peptides to elucidate the origins of biological activity is the theme of the paper contributed by Epand and coworkers, who are exploring how the biological activity of calcitonin analogues correlates with their biophysical properties. Lastly, Alix and coworkers present synergistic experimental and computational studies of the conformational preferences of short peptides responsible for the elasticity of elastin, a major component of the extracellular matrix.