Molecular mechanics studies of dermorphin |
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| Authors: | N Pattabiraman K R Sorensen R Langridge R S Bhatnagar V Renugopalakrishnan R S Rapaka |
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| Affiliation: | 1. School of Pharmacy and Dentistry, University of California, San Francisco, CA 94143 USA;2. Laboratory of Skeletal Disorders and Rehabilitation Department of Orthopaedic Surgery Harvard Medical School Boston, MA 02115 USA;1. Children''s Hospital Boston, MA 02115 USA;3. National Institute on Drug Abuse Rockville, MD 20857 USA;1. University of Natural Resources and Life Sciences, Vienna, Department of Water, Atmosphere and Environment, Institute of Soil Physics and Rural Water Management, Muthgasse 18, 1190 Vienna, Austria;2. Institute for Sustainable Agriculture, CSIC, Córdoba, Spain;1. Department of Chemistry, University of Pittsburgh, Pittsburgh PA, USA;2. LAAS-CNRS, Université Louis Pasteur, Strasbourg, France;1. Department of Physics, Sidho-Kanho-Birsha University, Purulia, 723104, West Bengal, India;2. Department of Chemistry, Ramakrishna Mission Residential College, Narendrapur, Kolkata, 103, West Bengal, India;3. Department of Physics, National Institute of Technology, Durgapur, 713209, West Bengal, India;4. Department of Physics, Balarampur College, P.O- Rangadih, Dist-Purulia, 723143, West Bengal, India;1. Sciences Po, Center for Research on Social Inequalities (CRIS), Paris, CNRS, France;2. Department of Social and Political Science, La Statale, University of Milan, Italy;3. Institut national d''etudes demographiques (INED), Paris, France;4. Economic and Social Research Institute, Dublin, Ireland;5. Universitat Ramon Llull, Esade, Spain |
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| Abstract: | Molecular mechanical simulations have been carried out on dermorphin. Presence of D-Ala2 at the N-terminus and L-Pro6 residue at the C-terminus indicated the probability of beta-turns. From the stereochemical considerations, three types- II', III' and V' - for the beta-turn at the N-terminus of the peptide and two types-I and III- for the C-terminus side of the peptide are possible. In our molecular mechanics calculations, we considered six folded and one extended conformations for dermorphin to asses the relative stabilities. Three of the six folded conformations are lower in energy and have the following general feature-similar in energy, three hydrogen bonds, semirigid beta-sheet segment and favorable Tyr1-Tyr5 interaction. The presence of beta-sheet structure might play a role in mu-receptor selective interaction of dermorphin. |
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