TAILIEUCHUNG - Báo cáo khoa học: Monitoring the prevention of amyloid fibril formation by a-crystallin Temperature dependence and the nature of the aggregating species

The molecular chaperone,a-crystallin, has the ability to prevent the fibril-lar aggregation of proteins implicated in human diseases, for example, amyloidbpeptide anda-synuclein. In this study, we examine, in detail, two aspects of a-crystallin’s fibril-suppressing ability: (a) its temperature dependence, and (b) the nature of the aggregating species with which it interacts. | ễFEBS Journal Monitoring the prevention of amyloid fibril formation by a-crystallin Temperature dependence and the nature of the aggregating species Agata Rekas1 2 Lucy Jankova3 David C. Thorn4 Roberto Cappai5 6 and John A. Carver4 1 Department of Chemistry University of Wollongong Australia 2 Institute for EnvironmentalResearch Australian Nuclear Science and Technology Organization Menai Australia 3 ATA Scientific Pty Ltd ANSTO Woods Centre Lucas Heights Australia 4 Schoolof Chemistry and Physics The University of Adelaide Australia 5 Department of Pathology Bio21 Institute The University of Melbourne Australia 6 MentalHealth Research Institute Melbourne Australia Keywords amyloid dual polarization interferometry NMR spectroscopy small heat shock protein temperature dependence Correspondence J. A. Carver School of Chemistry and Physics The University of Adelaide Adelaide South Australia 5005 Australia Fax 61 8 8303 4380 Tel 61 8 8303 3110 E-mail Received 22 May 2007 revised 12 October 2007 accepted 16 October 2007 doi The molecular chaperone a-crystallin has the ability to prevent the fibrillar aggregation of proteins implicated in human diseases for example amyloid b peptide and a-synuclein. In this study we examine in detail two aspects of a-crystallin s fibril-suppressing ability a its temperature dependence and b the nature of the aggregating species with which it interacts. First the efficiency of a-crystallin to suppress fibril formation in K-casein and a-synuclein increases with temperature despite their rate of fibrillation also increasing in the absence of a-crystallin. This is consistent with an increased chaperone ability of a-crystallin at higher temperatures to protect target proteins from amorphous aggregation GB Reddy KP Das JM Petrash WK Surewicz 2000 J Biol Chem 275 4565-4570 . Second dual polarization interferometry was used to monitor real-time a-syn-uclein aggregation in the presence

• Báo cáo khoa học
• Report medicine
• traditional medicine
• scientific reports
• Structural biochemistry
• bacteria
• chemical reaction
• medical knowledge
• medical research
• analysis of cytoplasmic
• oxidation
• Crystal structure
• hemoglobin
• medicine
• cell proliferation
• breast cancer
• gastric cancer
• hormone medicine
• tumor cells
• biochemical studies
• environmental medicine