John E. Maggio, Ph.D.


Ph.D., Harvard University, 1981

 

 

Research

The bioactive peptides are the largest and least understood class of intercellular messengers, carrying out a diverse set of functions in a wide variety of systems. Understanding bioactive peptides and their receptors, in the nervous system and elsewhere, is the general research goal in our group.

One system of interest is the tachykinin (substance P) family of peptides and receptors, which are involved in transmission of primary afferents and thus in pain and neurogenic inflammation. As the primary structures of both the ligands and their receptors are known, an excellent model system for peptide-protein interactions in signalling is available. Recently we have identified through photoaffinity labelling which regions of the peptide substance P interact with which regions of its G-protein-coupled receptor, a protein whose expression is upregulated a thousand-fold in some inflammatory diseases. Radioactive, fluorescent, and antibody probes of these receptors allow studies of desensitization and internalization in vivo and in vitro.

Another system under investigation is the process of amyloid formation in Alzheimer's disease (AD) and other amyloidoses. The characteristic lesion of AD is brain senile plaques formed mainly of the human amyloid peptide Ab, a *40-mer which occurs naturally in normal as well as AD brain. By reconstituting plaque growth (deposition of Ab at physiological concentrations onto authentic plaques) in vitro, we can characterize the process and identify conditions and components which enhance or inhibit its kinetics. Structure/activity studies have identified amino acids critical for amyloid deposition and active peptide analogues suitable for high resolution structure determination by nuclear magnetic resonance spectroscopy. The latter studies have further identified conformational elements essential to plaque deposition.

Another interest is the characterization of novel bioactive peptides from natural sources. A particularly rich source is the skin venom of certain neotropical frogs. The peptides found here include antibiotics and toxins as well as close analogs of discovered and yet undiscovered mammalian neuropeptides.

Publications

 

Department of Pharmacology and Cell Biophysics
University of Cincinnati
PO Box 670575 Cincinnati, OH 45267-0575
Phone: (513) 558-2366   Fax: (513) 558-1169

 

This page was developed by the Department of Pharmacology & Cell Biophysics and updated on 8-4-05. Please email us with any questions or comments. Copyright 2005, University of Cincinnati