کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2487468 | 1114418 | 2008 | 26 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
High-field solution NMR spectroscopy as a tool for assessing protein interactions with small molecule ligands
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
Drug interactions - تداخل داروییProtein structure - ساختار پروتئینStructure–activity relationship (SAR) - ساختار-فعالیت (SAR)Drug design - طراحی دارو NMR spectroscopy - طیف سنجی رزونانس مغناطیسی هستهHigh-throughput technologies - فن آوری های با توان بالاProteins - پروتئین هاProtein binding - پیوند پروتئین
موضوعات مرتبط
علوم پزشکی و سلامت
داروسازی، سم شناسی و علوم دارویی
اکتشاف دارویی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The ability of a small molecule to bind and modify the activity of a protein target at a specific site greatly impacts the success of drugs in the pharmaceutical industry. One of the most important tools for evaluating these interactions has been high-field solution nuclear magnetic resonance (NMR) because of its unique ability to examine even weak protein-drug interactions at high resolution. NMR can be used to evaluate the structural, thermodynamic and kinetic aspects of a binding reaction. The basis of NMR screening experiments is that binding causes a perturbation in the physical properties of both molecules. Unique properties of small and macromolecules allow selective detection of either the protein target or ligand, even in a mixture of compounds. This review outlines current methodologies for assessing protein-ligand interactions from the perspectives of the protein target and ligand and delineates the fundamental principles for understanding NMR approaches in drug research. Advances in instrumentation, pulse sequences, isotopic labeling strategies, and the development of competition experiments support the study of higher molecular weight protein targets, facilitate higher-throughput and expand the range of binding affinities that can be evaluated, enhancing the utility of NMR for identifying and characterizing potential therapeutics to druggable protein targets.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Pharmaceutical Sciences - Volume 97, Issue 11, November 2008, Pages 4670-4695
Journal: Journal of Pharmaceutical Sciences - Volume 97, Issue 11, November 2008, Pages 4670-4695
نویسندگان
Andria L. Skinner, Jennifer S. Laurence,