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Kinetic and Surface Properties of alpha-synuclein : Investigating the Difference between Pure Peptide and Phospholipid Including Aggregates

Nasir, Irem LU (2011) KEMN10 20111
Department of Chemistry
Abstract
Popular summary
Parkinson's Disease is a disorder caused by brain that affects patients' coordination, movement as well as causing tremor. The onset of Parkinson's Disease is found to be the
large fibrillar aggregates in the brain which consists mostly alpha-synuclein protein. The disease propagation has also been associated with membrane disruption. It is important to investigate the interaction of alpha-synuclein with lipid membranes since it gives an idea about how the things work in a cell.

In this project, the fibrillation kinetics and surface properties of alpha-synuclein in presence or without the presence of lipids are studied in model systems using several different techniques, including fluorescence spectroscopy, quartz... (More)
Popular summary
Parkinson's Disease is a disorder caused by brain that affects patients' coordination, movement as well as causing tremor. The onset of Parkinson's Disease is found to be the
large fibrillar aggregates in the brain which consists mostly alpha-synuclein protein. The disease propagation has also been associated with membrane disruption. It is important to investigate the interaction of alpha-synuclein with lipid membranes since it gives an idea about how the things work in a cell.

In this project, the fibrillation kinetics and surface properties of alpha-synuclein in presence or without the presence of lipids are studied in model systems using several different techniques, including fluorescence spectroscopy, quartz crystal microbalance with dissipation (QCM-D) and ellipsometry. It is found that the presence of anionic lipids makes fibrillation process faster than when protein without any additives in solution. Lipid to protein ratio is found out
to be inversely proportional to the time waited before fibrillation starts. Lastly, both the binding of fluorescent probes and the surface technique studies suggest that the aggregates that contain only peptide have different surface properties compared to the ones that contain lipids. (Less)
Abstract
Alpha-synuclein is a protein that has been found in Lewy bodies and Lewy neurites, which are filamentous aggregates that known are as the onset of Parkinson's Disease. The purpose of this study to investigate how the presence of phospholipid vesicles affect alpha-synuclein fibrillation different than when alpha-synuclein fibrillated in buffer, hydrophobicity during the aggregation process, monitored by fluorescence spectroscopy. The surface properties of different alpha-synuclein aggregates further investigated by two complementary adsorption techniques; namely quartz crystal microbalance with dissipation (QCM-D) and ellipsometry. Results revealed that the presence of lipid vesicles alters the fibrillation process as monitored with... (More)
Alpha-synuclein is a protein that has been found in Lewy bodies and Lewy neurites, which are filamentous aggregates that known are as the onset of Parkinson's Disease. The purpose of this study to investigate how the presence of phospholipid vesicles affect alpha-synuclein fibrillation different than when alpha-synuclein fibrillated in buffer, hydrophobicity during the aggregation process, monitored by fluorescence spectroscopy. The surface properties of different alpha-synuclein aggregates further investigated by two complementary adsorption techniques; namely quartz crystal microbalance with dissipation (QCM-D) and ellipsometry. Results revealed that the presence of lipid vesicles alters the fibrillation process as monitored with noncovalent dye ANS, while lipid containing aggregates are predicted to have less hydrophobicity than the ones contain pure alpha-synuclein. Accelearing trend has also been seen with different lipid mixtures, possessing the same charge. It is observed that lipid to protein ratio is inversely proportional to the lag time. Adsorption is more in pure peptide aggregates, however different type of experiments need to be done to be sure of the aggregate properties. (Less)
Please use this url to cite or link to this publication:
author
Nasir, Irem LU
supervisor
organization
course
KEMN10 20111
year
type
H2 - Master's Degree (Two Years)
subject
keywords
Nanokemi
language
English
id
3458454
date added to LUP
2013-02-11 11:29:11
date last changed
2013-02-11 11:50:46
@misc{3458454,
  abstract     = {Alpha-synuclein is a protein that has been found in Lewy bodies and Lewy neurites, which are filamentous aggregates that known are as the onset of Parkinson's Disease. The purpose of this study to investigate how the presence of phospholipid vesicles affect alpha-synuclein fibrillation different than when alpha-synuclein fibrillated in buffer, hydrophobicity during the aggregation process, monitored by fluorescence spectroscopy. The surface properties of different alpha-synuclein aggregates further investigated by two complementary adsorption techniques; namely quartz crystal microbalance with dissipation (QCM-D) and ellipsometry. Results revealed that the presence of lipid vesicles alters the fibrillation process as monitored with noncovalent dye ANS, while lipid containing aggregates are predicted to have less hydrophobicity than the ones contain pure alpha-synuclein. Accelearing trend has also been seen with different lipid mixtures, possessing the same charge. It is observed that lipid to protein ratio is inversely proportional to the lag time. Adsorption is more in pure peptide aggregates, however different type of experiments need to be done to be sure of the aggregate properties.},
  author       = {Nasir, Irem},
  keyword      = {Nanokemi},
  language     = {eng},
  note         = {Student Paper},
  title        = {Kinetic and Surface Properties of alpha-synuclein : Investigating the Difference between Pure Peptide and Phospholipid Including Aggregates},
  year         = {2011},
}