Modeling TRPV1, a Detector of Thermal and Chemical Stimuli, Producing Pain: No Capsaicin Sensation
| Autor: | S. Gottfried, E Barrett, Katherine J. Zappia, T Siy, A Hairston, J Dzwierzynski, M Zagloul, M Carrig, J David, S. Strandberg, C Rooney, Y Ahmad, M Thew, S Soczka, C. Feller, Andy D. Weyer, C. Scherrer, R Ryan, S Fleischmann, A Ahmad, E Schauer |
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| Rok vydání: | 2015 |
| Předmět: |
Chemistry
Chronic pain TRPV1 Stimulus (physiology) medicine.disease Biochemistry Transient receptor potential channel chemistry.chemical_compound Nociception nervous system Capsaicin Anesthesia Sensation Genetics Nociceptor medicine lipids (amino acids peptides and proteins) Molecular Biology Neuroscience Biotechnology |
| Zdroj: | The FASEB Journal. 29 |
| ISSN: | 1530-6860 0892-6638 |
| DOI: | 10.1096/fasebj.29.1_supplement.lb54 |
| Popis: | According to the Institute of Medicine, 100 million Americans suffer from chronic pain every year and the US spends over $500 billion trying to treat them. Pain begins as a stimulus that is detected by nociceptors, which are nerve fibers responsible for the detection of noxious mechanical, thermal, or chemical stimuli that give rise to pain sensations. These nociceptors transmit pain signals from the periphery to neurons in the spinal cord and brain. The Transient Receptor Potential Vanilloid 1 (TRPV1) is a nociceptive ion channel activated by capsaicin (the spicy component of hot peppers), heat, and endogenous pain molecules. Therefore, creating an inhibitor that partially blocks TRPV1 could treat chronic pain. The amino acids in the active site of TRPV1 are Y511, S512, M547, and T550. In addition, E600 controls the selectivity filter at the top gate of the channel and the hydrophobic seal mediated through I679 controls the lower gate. When capsaicin binds to the channel, a conformational change occurs t... |
| Databáze: | OpenAIRE |
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