Biomolecular Interfaces: Interactions, Functions and Drug Design
Latest Book by Ariel Fernandez
Springer International Publishing
Richard L. Moss Ph.D.
Rennebohm Professor of Cell and Regenerative Biology
Senior Associate Dean for Basic Research, Biotechnology and Graduate Studies
University of Wisconsin School of Medicine and Public Health
Madison, Wisconsin, USA
The book by Ariel Fernandez deals with a largely overlooked area of molecular biophysics that is likely to have strong impact on molecularly targeted medicine and drug design: the aqueous interface of a soluble protein. Foundational knowledge is presented in the first seven chapters and enables the reader to effectively tackle major problems in biophysics, such as the protein folding problem and the therapeutic disruption of protein–protein associations. These advances have been heralded by others, as is evident, for example, in a recent review published in Scientific American by Philip Ball . The remaining eight chapters deal with medical applications mostly centered on rational drug design guided by the interfacial patterns of the protein targets. Some of these advances involve reworking anticancer drugs to make them safer and less toxic and to control their specificity, all of which are reviewed in great detail. This novel type of design was enthusiastically received by eminent physician scientists such as Thomas Force (Vanderbilt University)  and was also covered in very promising terms for example in a review by Harvard oncologist George D. Demetri . Quoting Dr. Demetri: “The first generation of kinase-inhibitory drugs such as imatinib and sunitinib have already provided patients with life-saving therapeutic options, and with tools such as those described by Ariel Fernández et al., the future certainly looks bright for constructing ever-better agents that can be combined safely and effectively to manage, and eventually cure, many forms of human cancer.”
These seminal advances are further enriched in the book with a description of novel molecular design concepts that enable us to therapeutically disrupt protein–protein interfaces. This problem is considered to be a holy grail of molecular targeted therapy. Therapeutic opportunities stem from the advances described in the book. One illustration is provided in the potential treatment of heart failure by disrupting a myosin association with a myosin-regulatory protein (http://www.warf.org/documents/technology-summary/P120252US02.pdf)
an invention with a pending patent by this reviewer (Richard Moss) and Ariel Fernandez, the author of the book.
All in all, the book reports considerable conceptual novelty rooted in fundamental
knowledge that needs to find its way into the pharmaceutical discovery and
development pipeline, in particular in the hit-to-lead and lead optimization phases.
Paraphrasing George Demetri  we conclude that the approach by Prof. Ariel Fernández and coworkers holds great promise for customized development of rationally designed therapeutic agents.