The 18th biennial meeting of the International Society for Molecular Recognition (ISMR), Affinity 2009, took place, on 12–16 July 2009 at the University of Iceland in Reykjavik. The idea of hosting the meeting in Reykjavík was originally suggested at the Affinity 2005 meeting in Uppsala and later adopted by the ISMR Council.

The timing of the meeting created some difficulties. The international financial crisis of 2008, which included the virtual collapse of the Icelandic banking system in October 2008, caused a certain degree of reluctance to attend a meeting in Iceland. Furthermore, the transfer of funds to Iceland by any route was for some months problematic. On the other hand, a drastic fall in the value of the Icelandic króna had a favorable effect on the dollar and euro, so participation and accommodation became more affordable. After a slow start, registration eventually picked up and about 90 participants came to Reykjavík from all over the world to a meeting that turned out to be very successful.

The theme of the scientific program had been set as “Exploring the interactome—the technology and biology of molecular recognition,” with the idea of giving the meeting an even wider scope than previous meetings, while keeping a balance between basic research, technology, and applications. The format of the meeting was in the tradition of previous ones, which commenced with a welcome reception, followed by an inaugural lecture, delivered by Nathan Sharon, entitled, “Lectins: Carbohydrate-Specific Reagents and Biological Recognition Molecules.”

Several scientific sessions featuring excellent poster presentations, keynote lectures, the Award-giving ceremonies, and a conference dinner were among the other traditional highlights at Affinity 2009. The first session, chaired by Gideon Fleminger, was entitled “Fundamental Nature of Biological Interactions.” The second, “In vitro Design and Selection of Affinity Probes,” was chaired by Klaus Mosbach. Hörður Filippusson chaired the third session, entitled “Mapping and Screening of the Interactome.” Mathias Uhlén chaired the fourth session on “Affinity Proteomics and Interactomics.” The fifth session, “Affinity for Therapy and Structure-based Discovery,” was chaired by George Ehrlich. Richard Willson chaired the seventh session on “Affinity in Nanobiotechnology and Molecular Devices,” and the final session, chaired by Hörður Filippusson, was devoted to other topics relevant to the main theme of the conference. In addition to the lectures, a total of 43 posters were on display throughout the conference.

In a special session for the Pierce Affinity Award Presentation, Meir Wilchek, the Chairman of the ISMR Pierce Award Committee introduced the recipient of the award, Rudi Aebersold, for his pioneering work in the analysis of cell networks using modern mass spectrometric techniques. The title of Rudi´s lecture was “Systems Biology: Networks of Interacting Molecules.”

The Younger Investigators Award sponsored by Roche was organized by A. Cecilia Roque, Abid Hussain, and George Ehrlich. Eleven younger investigators, who received awards for their presentations and active participation, are as follows: Alexander Riechers from Gemany, Sandip Shelke and Haraldur Garðarsson from Iceland, Ana Carina Silva, Angela Sousa, Ana Pina, Claudia Silva, Claudia Vistas, and Brigitte Tomé from Portugal, Óttar Rolfsson from UK, and Johannes Preiner from Austria.

The meeting was closed by announcing the venue of Affinity 2011. It will be held in Faro, Portugal on 19–23 June 2011 and organized by Guilherme N. M. Ferreira.

The 14 peer-reviewed articles published in this special issue span the spectrum of topics presented at Affinity 2009 and cover numerous aspects of affinity-based science and technology. The first part of the volume is dedicated to Affinity technologies, opening with a review by Sousa et al., which investigates features of protein–DNA interaction and their utilization in advanced affinity chromatographic methods. The following article, also by Sousa et al., describes the purification of small, non-coding 6S RNA from E. coli using histidine affinity chromatography. It is followed with an article by Ed Bayer's group who developed a new dockerin-based affinity tag and exemplified its application for purification of a broad variety of target proteins on cellulose affinity columns. The next article by Roque et al. describes the effects of gum-arabic coated magnetic nanoparticles on the growth of various cell lines, while Nicole Schneiderhan and her group describe the use of a miniaturized bead assay to examine the involvement of different Rho GTPases in cellular function.

The subsequent article by Pengo et al. demonstrates the novel application of immunoaffinity matrices, combined with avidin–biotin interactions to prepare protein complexes for use in immunometric methods, where it is essential to preserve the immunoreactivity of each component. The next three articles also deal with antibodies and their binding properties. In the first article, Danièle Altschuh and her group show that the binding of CDR-derived peptides is mechanistically different from that of high-affinity parental antibodies. The following article by Azevedo et al. describes the application of phenyl boronate matrices for capturing human monoclonal antibodies from cell culture supernatants. Finally, Kamalanathan et al. describe a unique catalytic activity of IgM antibodies from rheumatoid arthritis patients' sera, analyzed by specific synthetic peptide substrates.

The next part of this volume is dedicated to the study of mechanisms of molecular interactions using advanced monitoring systems. The first article by Sekatskii et al. describes the use of atomic force spectroscopy to elucidate the interaction of barnase and barstar at the single molecule level. Chtcheglova et al. in the following article used AFM Functional Imaging to visualize cadherin on vascular endothelial cells and learn about its function in the formation of cellular linkages. Another advanced technology used to study protein interactions at the molecular level is through piezoelectric and acoustic devices. The article by Helga Schnerr describes the application of a label-free method, based on resonant acoustic profiling technology for real-time analysis of biomolecular interactions as an efficient way to optimize the development and production process of recombinant proteins. The next article by Nicholls et al. investigates the environmental-dependent interactions of Warfarin isomers with specific proteins using a variety of physical methods. The volume concludes with an article from the group of Barbara Andrews, and Juan Asenjo, who delineate a mathematical model for protein purification, which simulates and optimizes separation conditions for affinity chromatography.

We wish to thank all the contributors to this volume, as well as the 33 reviewers who spared neither time nor effort for shaping and polishing the manuscripts presented in the following pages. Thanks are also due to the editors of the Journal of Molecular Recognition, the Editor in Chief Prof. Marc H.V. Van Regenmortel and the Executive Commissioning Editor, Dr Martin Rothlisberger, for the continuing support of the special relationship between the Journal and ISMR and for publishing these proceedings. Especially appreciated is the assistance of the JMR staff, in particular, Ms Amanda Smith, Charlotte Pearson, Catherine Delos Reyes, and Mr Stefan Koernig, who helped us in overcoming difficulties encountered in the editorial work and achieving the final form of this volume. Special thanks are also due to Ed Bayer and Meir Wilchek for reviewing, polishing, and bettering this Editorial article.

The ISMR and meeting organizers are grateful to the following sponsors for their support: the University of Iceland and the Science Institute, TTP Labtech, Eco Chemie BV, Pierce (Thermo Fisher Scientific), Hoffmann-La Roche, and GE Healthcare.

The aim of the Affinity series, which dates back to the first meeting in Liverpool, UK, in 1975, was to create a platform where Academic, Industrial and Government scientists with a common interest in the study of Affinity and Biorecognition could share their ideas, observations and understanding. The ISMR was launched during the fifth meeting on Affinity Chromatography and Biorecognition, held in Annapolis, MD, in 1983, as a result of its success and the remarkable impact of the four preceding meetings. The Journal of Molecular Recognition followed in 1988.

The contributions to science and technology made by members of the ISMR have had a lasting impact on how materials, such as natural and recombinant proteins, are prepared, characterized, analyzed, and used.

This volume is dedicated to the memory of Ephraim Katchalski-Katzir (1916–2009), who played a significant role in founding and shaping ISMR. Ephraim was a pioneer Scientist in biochemistry, biophysics, and biotechnology, devoting his time to the study of protein structure and function, including the biophysical basis for protein interactions. He founded and headed the Biophysics Department at the Weizmann Institute in Rehovot and the Department of Biotechnology at the Tel Aviv University. Ephraim was also a renowned statesman who served his country as the fourth President of Israel.

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Ephraim Katchalski-Katzir