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Effects of solution parameters on th...

Vessely, Christina Regina.

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Effects of solution parameters on the adsorption of proteins at interfaces.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Effects of solution parameters on the adsorption of proteins at interfaces./
作者:	Vessely, Christina Regina.
面頁冊數:	173 p.
附註:	Adviser: John F. Carpenter.
Contained By:	Dissertation Abstracts International67-06B.
標題:	Chemistry, Pharmaceutical. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3219964
ISBN:	9780542734120

Effects of solution parameters on the adsorption of proteins at interfaces.
Vessely, Christina Regina.

Effects of solution parameters on the adsorption of proteins at interfaces. - 173 p.

Adviser: John F. Carpenter.

Thesis (Ph.D.)--University of Colorado Health Sciences Center, 2006.

Proteins adsorb at interfaces due to their amphiphilic nature, with consequences including decreased activity and the promotion of aggregation in bulk solution. Prevention of adsorption is usually a priority in therapeutic protein product development, although there are applications (drug delivery systems, vaccines) which actually require adsorption of proteins to surfaces.

ISBN: 9780542734120Subjects--Topical Terms:

550957
Chemistry, Pharmaceutical.

Effects of solution parameters on the adsorption of proteins at interfaces.
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245 1 0 $a Effects of solution parameters on the adsorption of proteins at interfaces.
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500 $a Adviser: John F. Carpenter.
500 $a Source: Dissertation Abstracts International, Volume: 67-06, Section: B, page: 3148.
502 $a Thesis (Ph.D.)--University of Colorado Health Sciences Center, 2006.
520 $a Proteins adsorb at interfaces due to their amphiphilic nature, with consequences including decreased activity and the promotion of aggregation in bulk solution. Prevention of adsorption is usually a priority in therapeutic protein product development, although there are applications (drug delivery systems, vaccines) which actually require adsorption of proteins to surfaces.
520 $a This thesis is an investigation into protein adsorption at a variety of interfaces. The focus of this work centers on the promotion of interfacial adsorption. However, the resulting information is applicable to both promotion and prevention of adsorption under a variety of circumstances. Topics covered include the adsorption of model proteins to a magnetic targeted particulate drug delivery system, the behavior of beta-casein at the air-water interface, and the development of a multivalent recombinant subunit vaccine against Botulinum Neurotoxin. In the drug delivery study, protein adsorption, desorption, and activity were monitored under a variety of solution conditions. The study of beta-casein included utilized surface specific techniques (interfacial rheology, atomic force microscopy, and IRRAS) to monitor both macroscopic and microscopic changes to protein interfacial behavior. The vaccine project focused first on the optimization of adsorption profiles of toxin to aluminum salt adjuvants. The stability of the adsorbed antigens was then monitored by assessing changes to total mass adsorbed, chemistry of the complex, and protein conformation over time.
520 $a The results of this work indicate that protein adsorption is driven by multiple forces, including electrostatic and hydrophobic interactions. The dominant force depends on protein characteristics including protein surface hydrophobicity, tendency to unfold upon adsorption, interfacial characteristics, and solution parameters including pH, ionic strength, temperature, and the inclusion of stabilizers such as sugars or surfactants. The optimization of solution conditions can result in greater yields in the processing of therapeutic proteins, as well as in the development of more stable adsorbed protein products.
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