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Protein adsorption on solid surfaces.
~
Kaewtathip, Sarawut.
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Protein adsorption on solid surfaces.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
Protein adsorption on solid surfaces./
作者:
Kaewtathip, Sarawut.
面頁冊數:
227 p.
附註:
Source: Dissertation Abstracts International, Volume: 65-07, Section: B, page: 3577.
Contained By:
Dissertation Abstracts International65-07B.
標題:
Engineering, Chemical. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3140489
ISBN:
9780496876303
Protein adsorption on solid surfaces.
Kaewtathip, Sarawut.
Protein adsorption on solid surfaces.
- 227 p.
Source: Dissertation Abstracts International, Volume: 65-07, Section: B, page: 3577.
Thesis (Ph.D.)--University of Southern California, 2004.
Protein adsorption is crucial in many processes. To name a few, it is the underlying principle of the fouling of biomaterials implants as well as the corrosion of marine structures. Although much effort has been placed on the topic and much knowledge has been gained, many issues in protein adsorption still remain a mystery. A glimpse of the true mechanism of this complex process is not within sight. The objective of this study is to gain further understanding on the mechanism of protein adsorption so that the rate and the extent of protein adsorption as well as the conformation change can be systematically controlled. FTIR/ATR is employed to monitor the adsorption kinetics of four proteins including BSA, lysozyme, IgG, and fibrinogen at various conditions on various surfaces. The results constitute the central part of this study. Simulation is also performed and the results are used to develop a model.
ISBN: 9780496876303Subjects--Topical Terms:
1018531
Engineering, Chemical.
Protein adsorption on solid surfaces.
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Protein adsorption is crucial in many processes. To name a few, it is the underlying principle of the fouling of biomaterials implants as well as the corrosion of marine structures. Although much effort has been placed on the topic and much knowledge has been gained, many issues in protein adsorption still remain a mystery. A glimpse of the true mechanism of this complex process is not within sight. The objective of this study is to gain further understanding on the mechanism of protein adsorption so that the rate and the extent of protein adsorption as well as the conformation change can be systematically controlled. FTIR/ATR is employed to monitor the adsorption kinetics of four proteins including BSA, lysozyme, IgG, and fibrinogen at various conditions on various surfaces. The results constitute the central part of this study. Simulation is also performed and the results are used to develop a model.
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Certain experimental results reveal that protein adsorption is completely irreversible at low bulk concentrations and become partially reversible at higher bulk concentrations. There is a greater extent of structural rearrangement upon adsorption at lower bulk concentration. There is also a greater extent of structural rearrangement on a more hydrophobic surface. When the pH is varied, the maximum adsorption occurs around the isoelectric point. There is an asymmetrical sensitivity in adsorption with respect to pH change. Buffers appear to have overwhelming effects on protein adsorption. Tris-HCl promotes the adsorption while PBS suppresses it. Except for lysozyme, considerable differences in the protein adsorbed amounts were found under the two buffers environments. Different concentrations of the same buffer also constitute different adsorption behaviors. Under Tris-HCl environment, gel-like IgG aggregate was observed and a drastic change in the secondary structures was revealed. Greater reversibility of adsorption was observed under PBS environment.
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We have also presented the results from lattice simulation. The generally accepted steps representing the net results of the many-body interactions in the adsorption process are accounted for. The results are used to build a mathematical model for fitting the experimental data. The trends on the parameters are discussed.
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