The investigation of membrane binding by amphibian peptide agonists of CCK2R using 31P and 2H solid-state NMR |
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| Institution: | 1. Department of Chemistry, The University of Adelaide, South Australia 5005, Australia;2. School of Chemistry, Bio21 Institute, University of Melbourne, Victoria 3010, Australia;1. Intervention Division, Taiyuan City Centre Hospital, Taiyuan 030001, China;2. Cadre Health Centre, Qinghai People''s Hospital, Xining 810000, China;3. Department of Senile Internal Medicine, Second Hospital of Shanxi Medical University, Taiyuan 030001, China;1. Department of Physiology, Medical College of Nanchang University, Bayi Road 461, Nanchang, Jiangxi 330006, China;2. Key Laboratory of Poyang Lake Environmental and Resource Utilization, Ministry of Education, School of Environmental and Chemical Engineering, Nanchang University, Nanchang, Jiangxi 330029, China;3. Medical Experimental Teaching Department, Nanchang University, Nanchang 330031, China;1. CNR Institute of Clinical Physiology, Laboratory of Cardiovascular Biochemistry, Pisa, Italy;2. CNR Institute of Clinical Physiology, Milan, Italy;3. Cardiovascular Department, Niguarda Ca’ Granda Hospital, Milan, Italy;1. Centre National de la Recherche Scientifique, Institut de Pharmacologie et de Biologie Structurale, F-31077 Toulouse, France;2. Université de Toulouse, Université Paul Sabatier, Institut de Pharmacologie et de Biologie Structurale, F-31077 Toulouse, France;1. CURE/Digestive Diseases Center and Center for Neurobiology of Stress, Department of Medicine, Digestive Diseases Division, University of California at Los Angeles, and VA Greater Los Angeles Health Care System, Los Angeles, CA, USA;2. Tsumura Research Laboratories, Ibaraki, Japan;3. Department of Gastroenterology and Hepatology, Saitama Medical Center, Saitama Medical University, Saitama, Japan |
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| Abstract: | It has been proposed that some neuropeptides may be anchored to the cell membranes prior to attaching to the adjacent active sites of transmembrane receptors. The three amphibian skin neuropeptides signiferin 1 RLCIPYIIPC(OH)] (smooth muscle active and immunomodulator), riparin 1.1 RLCIPVIFPC(OH)] (immunomodulator) and rothein 1 SVSNIPESIGF(OH)] (immunomodulator) act via CCK2 transmembrane receptors. A combination of 31P and 2H solid state NMR studies of each of these three peptides in eukaryotic phospholipid models at 25 °C shows that rothein 1 does not interact with the membrane at all. In contrast, both of the cyclic disulfides signiferin 1 and riparin 1.1 interact with phospholipid head groups and partially penetrate into the upper leaflet of the model bilayer, but to different extents. These interactions are not sufficiently effective to cause disruption of the lipid bilayer since the peptides are not antimicrobial, anticancer, antifungal nor active against enveloped viruses. |
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| Keywords: | Signiferin 1 Riparin 1 1 Rothein 1 3D NMR structures Smooth muscle activity Immunological activity Trans membrane CCK2 receptors Binding to eukaryotic model phospholipids |
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