Structural stability of amyloid fibrils of [beta]2-microglobulin in comparison with its native fold

@article{citeulike:3017516, abstract = {Among various amyloidogenic proteins, [beta]2-microglobulin ([beta]2-m) responsible for dialysis-related amyloidosis is a target of extensive study because of its clinical importance and suitable size for examining the formation of amyloid fibrils in comparison with protein folding to the native state. The structure and stability of amyloid fibrils have been studied with various physicochemical methods, including H/D exchange of amyloid fibrils combined with dissolution of fibrils by dimethylsulfoxide and NMR analysis, thermodynamic analysis of amyloid fibril formation by isothermal calorimetry, and analysis of the effects of pressure on the structure of amyloid fibrils. The results are consistent with the view that amyloid fibrils are a main-chain-dominated structure with larger numbers of hydrogen bonds and pressure-accessible cavities in the interior, in contrast to the side-chain-dominated native structure with the optimal packing of amino acid residues. We consider that a main-chain dominated structure provides the structural basis for various conformational states even with one protein. When this feature is combined with another unique feature, template-dependent growth, propagation and maturation of the amyloid conformation, which cannot be predicted with Anfinsen's dogma, take place.}, author = {Chatani, Eri and Goto, Yuji }, booktitle = {Dialysis-related amyloidosis: from molecular mechanisms to therapies}, citeulike-article-id = {3017516}, doi = {http://dx.doi.org/10.1016/j.bbapap.2005.08.002}, journal = {Biochimica et Biophysica Acta (BBA) - Proteins \& Proteomics}, keywords = {amyloid, experiment, microglobulin, stability}, month = {November}, number = {1}, pages = {64--75}, posted-at = {2008-07-18 11:43:15}, priority = {2}, title = {Structural stability of amyloid fibrils of [beta]2-microglobulin in comparison with its native fold}, url = {http://dx.doi.org/10.1016/j.bbapap.2005.08.002}, volume = {1753}, year = {2005} }

TY - JOUR ID - citeulike:3017516 L3 - citeulike-article-id:3017516 TI - Structural stability of amyloid fibrils of [beta]2-microglobulin in comparison with its native fold T2 - Dialysis-related amyloidosis: from molecular mechanisms to therapies JF - Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics VL - 1753 IS - 1 SP - 64 EP - 75 N2 - Among various amyloidogenic proteins, [beta]2-microglobulin ([beta]2-m) responsible for dialysis-related amyloidosis is a target of extensive study because of its clinical importance and suitable size for examining the formation of amyloid fibrils in comparison with protein folding to the native state. The structure and stability of amyloid fibrils have been studied with various physicochemical methods, including H/D exchange of amyloid fibrils combined with dissolution of fibrils by dimethylsulfoxide and NMR analysis, thermodynamic analysis of amyloid fibril formation by isothermal calorimetry, and analysis of the effects of pressure on the structure of amyloid fibrils. The results are consistent with the view that amyloid fibrils are a main-chain-dominated structure with larger numbers of hydrogen bonds and pressure-accessible cavities in the interior, in contrast to the side-chain-dominated native structure with the optimal packing of amino acid residues. We consider that a main-chain dominated structure provides the structural basis for various conformational states even with one protein. When this feature is combined with another unique feature, template-dependent growth, propagation and maturation of the amyloid conformation, which cannot be predicted with Anfinsen's dogma, take place. KW - amyloid KW - experiment KW - microglobulin KW - stability AU - Chatani, Eri AU - Goto, Yuji PY - 2005/11/10/ UR - http://dx.doi.org/10.1016/j.bbapap.2005.08.002 ER -