European Peptide Society

The Journal of Peptide Science will soon publish a selection of papers presented at the 2nd International Congress on Natural Peptides to Drugs, which took place in Zermatt, Switzerland from in April 2006.

Philippe Bulet acted as a Guest Editor for this issue. Some of the articles were published on Wiley Interscience EarlyView at the end of July 2007.

We are pleased to provide free access to two articles in this issue:

Peptides as tools and drugs for immunotherapies
Alain Beck, Christine Klinguer-Hamour, Marie-Claire Bussat, Thierry Champion, Jean-François Haeuw, Liliane Goetsch, Thierry Wurch, Masae Sugawara, Alain Milon, Alain Van Dorsselaer, Thien Nguyen, Nathalie Corvaia

Abstract
Peptides are essential tools for discovery and pre-clinical and pharmaceutical development of viral and cancer vaccines (active immunotherapies) as well as for therapeutic antibodies (passive immunotherapies). They help to trigger and analyze immune responses at a molecular level (B-cell, T-helper and CTL epitopes). They contribute largely to the design of new vaccine candidates and to the generation of monoclonal antibodies. They are also valuable analytical reference compounds for the structural characterisation by liquid chromatography and mass spectrometry of recombinant proteins used as biopharmaceuticals. As for other therapeutic applications, formulation, solubilisation, batch consistency and stability, issues have to be addressed to allow the pre-clinical and clinical development of this class of compounds as immunotherapeutic drugs. In the present review, three case studies dealing with (i) the design and the characterisation of Respiratory Syntycial Virus subunit vaccines, (ii) peptide-based melanoma vaccines, and (iii) therapeutic monoclonal antibodies, all investigated in clinical trials, are reported and discussed.
Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd. 
 

Multivalency - a way to enhance binding avidities and bioactivity - preliminary applications to EPO
Oscar Vadas, Keith Rose

Abstract
Multivalency has advantages over monovalency for binding interactions and even for activity. In particular, avidity is higher since the off-rate of a multivalent species is much slower than that of a monomer. This is particularly profitable for ligand-binding receptors that require dimerization for activity, such as the receptor of erythropoietin (EPOR). Peptides that mimic the action of erythropoietin (EPO) have been described with no sequence similarity with the human hormone: erythropoietin mimetic peptide (EMP) and EPO receptor peptide (ERP). These two peptides have similar activity but interact through different sites on the EPOR. Here, we describe the construction of several new synthetic homo- and hetero-dimers based on EMP-ERP sequences. To link the monomeric molecules together, several monodisperse polyamide linkers of different lengths were synthesized with dialdehyde functionalities. Chemoselective oxime chemistry was used to obtain homogeneous constructs. Certain chemical incompatibilities were dealt with via a protection approach. The oximes are stable under normal conditions and so lend themselves to biological testing.
Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.