عنوان :
مطالعه ي بر همكنش هاي بين باز شيف هاي چهار دندانه اي[N2S2] و آلبومين سرم انساني و طراحي محاسباتي مشتقات تريپروستاتين -A و دي كتو پي پرازين به عنوان بازدارنده هاي جديد Ba-توبولين
گرايش تحصيلي :
شيمي فيزيك
محل تحصيل :
اصفهان: دانشگاه صنعتي اصفهان، دانشكده شيمي
صفحه شمار :
شانزده،132ص.: مصور،جدول،نمودار﴿رنگي﴾
يادداشت :
ص.ع.به فارسي و انگليسي
استاد راهنما :
يوسف غايب، عبدالخالق بردبار
توصيفگر ها :
داكينگ مولكولي , شبيه سازي ديناميك مولكولي , طراحي دارو , 2و5 دي كتو پرازين
تاريخ نمايه سازي :
25/4/93
استاد داور :
بيژن نجفي، تقي خياميان، داود عاجلو
كد ايرانداك :
ID647 دكتري
چكيده انگليسي :
150 Binding Studies of Human Serum Albumin with Tetradentate N2S2 Schiff Base Ligands And Computational Design of Tryprostatin A and Diketopiperazine Derivatives as Novel Tubulin Inhibitors Najmeh Fani n fani@ch iut ac ir May 2014 Department of Chemistry Isfahan University of Technology 84156 83111 Isfahan Iran 1st Supervisor Yousef Ghayeb E mail ghayeb@cc iut ac ir 2nd Supervisor Abdol Khalegh Bordbar E mail bordbar@chem ui ac ir Department Graduate Coordinator Alireza Najafi Department of Chemistry Isfahan University of Technology Isfahan 84156 83111 Iran Department of Chemistry University of Isfahan Isfahan 81746 73441 Iran Abstract In the first part of this work the interactions of three Schiff bases with human serum albumin HSA have been investigated by different kinds of molecular modeling and spectroscopic techniques Molecular docking study indicated that all Schiff bases bind to the subdomain IB of HSA Molecular dynamics results suggested that all Schiff bases can interact with HSA without affecting the secondary structure of HSA but probably with a slight modification of its tertiary structure Furthermore the experimental data suggested that all Schiff bases demonstrated a significant binding affinity to HSA and the process is enthalpy driven In the second part docking tools were utilized in order to design of novel Tubulin Inhibitors For this purpose more than one hundred derivatives of TPS A were designed and the interactions of them with tubulin were analyzed Thirteen designed analogous among them as the best docked compounds were selected on the basis of binding energy Moreover docking tools were utilized in order to study the binding properties of a series of proline based 2 5 diketopiperazine about 500compounds in the binding site of tubulin Results revealed the stronger anti tubulin activity of twenty compounds among them in comparison with tryprostatin A as a well known tubulin inhibitor Keywords Molecular docking Molecular dynamics simulation Spectroscopic techniques Schiff base Human serum albumin Tubulin inhibitors
استاد راهنما :
يوسف غايب، عبدالخالق بردبار
استاد داور :
بيژن نجفي، تقي خياميان، داود عاجلو
