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27
structure as −helix/random coil. Intramolecular -sheet peak usually centers around
1635-1638 cm-1 for BSA, IgG and fibrinogen. For lysozyme, intermolecular -sheet
exhibits two peaks, at 1633 and 1642 cm-1. These are combined and identified as
intermolecular -sheet. In graphical representation, for the sake of clarity, we show
only the three principal secondary structures: -helix/random coil, -sheet
(combination of intermolecular and intramolecular -sheets) and turns. Side chain
structures make minor contribution and are relatively stable and are therefore not
shown.
Table 2.3. Amide I spectral band positions (cm-1) of adsorbed BSA, IgG, fibrinogen
and lysozyme on Ge surface
2.3.2.1 Secondary Structures as Function of Adsorption Time
Fig. 2.6 shows the time evolution of the three main secondary structural
components ( -helix/random-coil, -sheet and turn) of adsorbed BSA, IgG, fibrinogen,
side
chain
intermolecular
-sheet
intramolecular
-sheet
-helix/
random coil
turn
BSA 1615±1.5 1626±0.3
1690±1.2
1637±0.3
1651±0.4
1661±1.0
1675±0.7
IgG 1615±1.5 1626±0.3
1690±1.2
1637±0.3
1651±0.4
1661±1.0
1675±0.7
Fibrinogen 1618±0.5
1685±0.3
1635±0.1
1646±0.8
1653±0.3
1666±0.4
1673±0.4
Lysozyme 1622±0.1
1691±0.8
1633±0.2
1642±0.4
1654±0.1 1674±0.4
1683±0.5
Object Description
| Title | Experimental study and atomic simulation of protein adsorption |
| Author | Wei, Tao |
| Author email | twei2004@gmail.com; dnaafm@yahoo.com.cn |
| Degree | Doctor of Philosophy |
| Document type | Dissertation |
| Degree program | Chemical Engineering |
| School | Viterbi School of Engineering |
| Date defended/completed | 2008-07-29 |
| Date submitted | 2008 |
| Restricted until | Unrestricted |
| Date published | 2008-10-07 |
| Advisor (committee chair) | Shing, Katherine |
| Advisor (committee member) |
Nakano, Aiichiro Goo, Edward K. |
| Abstract | The studies of protein adsorption at solid-liquid interface are important in various applications. Multilayer and irreversible adsorption behaviors are commonly observed. In this work, protein adsorption behavior at the solid-liquid interface was investigated by a combination of experimental Fourier transform infrared/attenuated total reflectance (FTIR/ATR) studies and computer simulations: Molecular Dynamics (MD) simulation and hybrid Genetic-Algorithm (GA) schemes.; BSA, lysozyme, IgG and fibrinogen adsorption was studied with FTIR/ATR in tris(hydroxymethyl)-aminomethane hydrochloride (Tris-HCl) and phosphate buffered saline (PBS) buffers on a Ge surface. Buffer choice was shown to drastically affect adsorption kinetics. In comparison with Tris-HCl, PBS buffer depresses the adsorption of BSA, IgG and fibrinogen in the prolonged quasi-linear kinetic region while lysozyme adsorption is relatively insensitive to buffer choice. Buffer concentration can also significantly affect protein adsorption. The secondary structures in the adsorbed phase are generally quite different from the bulk structure; however, buffer choice has negligible effect on structural evolution. Significant secondary structure changes occur during adsorption. The secondary structures in the adsorbed phase are inhomogeneous. The role of phosphate ions in PBS buffer and their effect on protein adsorption are rather complex. Phosphate ions adsorb competitively against protein molecules and their deprotonation equilibrium can be altered at the solid-liquid interface due to the adsorbed protein.; The effect of surface on adsorption is examined by adsorbing IgG on various polymer-coated surfaces. IgG adsorption is higher on more hydrophobic surface. IgG molecules adsorbed in layers near hydrophilic solid surfaces suffer less secondary structure changes.; The behavior of lysozyme during adsorption on a hydrogen-terminated Si surface (Si-H) is studied using MD simulations. Although atomistic simulations are highly time-consuming for direct observations of complete secondary structure changes, indications of molecular deformations are observed over nanosecond simulation time scale. Lysozyme molecule undergoes deformation onto the Si-H surface, as is evidenced by the reduction in the volume, the increase in solvent accessible surface area, the change of the overall shape, and certain amount of alteration in secondary structures. The main α-helix domains experience some loss while the beta-sheet domains remain almost intact. The hydrophobic character of the surface is believed to contribute to the loss of the organized structures of the amino residues in close proximity to the surface.; An efficient hybrid GA/spatial-grid method was developed to search for low adsorption-energy orientations and locations of a protein molecule on a solid surface. The surface and the protein molecule are treated as rigid bodies, whereas the bulk fluid is represented by spatial grids. The hybrid search procedure consists of two interlinked loops. In 1st loop (A), a GA is employed to identify promising regions for the global energy minimum, whereas a local optimizer with the derivative-free Nelder-Mead method is used to search for the lowest-energy orientation within the identified regions. In 2nd loop (B), new population is generated and competitive solution from loop A is improved. The switching between two loops is adaptively controlled by similarity analysis. We test the method for lysozyme adsorption on a hydrophobic Si-H (110) surface in implicit water. The hybrid search method was shown to have faster convergence and better solution accuracy compared with the conventional GA, which suffered from premature convergence. |
| Keyword | protein adsorption; FTIR/ATR; MD simulation; hybrid genetic algorithm |
| Language | English |
| Part of collection | University of Southern California dissertations and theses |
| Publisher (of the original version) | University of Southern California |
| Place of publication (of the original version) | Los Angeles, California |
| Publisher (of the digital version) | University of Southern California. Libraries |
| Provenance | Electronically uploaded by the author |
| Type | texts |
| Legacy record ID | usctheses-m1641 |
| Contributing entity | University of Southern California |
| Rights | Wei, Tao |
| Repository name | Libraries, University of Southern California |
| Repository address | Los Angeles, California |
| Repository email | cisadmin@lib.usc.edu |
| Filename | etd-Wei-2367 |
| Archival file | uscthesesreloadpub_Volume14/etd-Wei-2367.pdf |
Description
| Title | Page 43 |
| Contributing entity | University of Southern California |
| Repository email | cisadmin@lib.usc.edu |
| Full text | 27 structure as −helix/random coil. Intramolecular -sheet peak usually centers around 1635-1638 cm-1 for BSA, IgG and fibrinogen. For lysozyme, intermolecular -sheet exhibits two peaks, at 1633 and 1642 cm-1. These are combined and identified as intermolecular -sheet. In graphical representation, for the sake of clarity, we show only the three principal secondary structures: -helix/random coil, -sheet (combination of intermolecular and intramolecular -sheets) and turns. Side chain structures make minor contribution and are relatively stable and are therefore not shown. Table 2.3. Amide I spectral band positions (cm-1) of adsorbed BSA, IgG, fibrinogen and lysozyme on Ge surface 2.3.2.1 Secondary Structures as Function of Adsorption Time Fig. 2.6 shows the time evolution of the three main secondary structural components ( -helix/random-coil, -sheet and turn) of adsorbed BSA, IgG, fibrinogen, side chain intermolecular -sheet intramolecular -sheet -helix/ random coil turn BSA 1615±1.5 1626±0.3 1690±1.2 1637±0.3 1651±0.4 1661±1.0 1675±0.7 IgG 1615±1.5 1626±0.3 1690±1.2 1637±0.3 1651±0.4 1661±1.0 1675±0.7 Fibrinogen 1618±0.5 1685±0.3 1635±0.1 1646±0.8 1653±0.3 1666±0.4 1673±0.4 Lysozyme 1622±0.1 1691±0.8 1633±0.2 1642±0.4 1654±0.1 1674±0.4 1683±0.5 |
