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http://hdl.handle.net/123456789/5746
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DC Field | Value | Language |
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dc.contributor.author | Nsiah, Francis | - |
dc.contributor.author | McDermott, Mark T. | - |
dc.date.accessioned | 2021-07-27T10:05:59Z | - |
dc.date.available | 2021-07-27T10:05:59Z | - |
dc.date.issued | 2015 | - |
dc.identifier.issn | 23105496 | - |
dc.identifier.uri | http://hdl.handle.net/123456789/5746 | - |
dc.description | 21p:, ill. | en_US |
dc.description.abstract | The adsorption characteristics of human fibrinogen (HFG) on surfaces with well-controlled chemistries have been studied using infrared reflection absorption spectroscopy. The surfaces examined in this study provide the experimental basis for exploring fundamental non-covalent intermolecular forces that dominate protein adsorption processes. Comparisons were drawn between fibrinogen and non-specifically adsorbed bovine IgG (bIgG) as well as structurally rigid lysozyme (LYS) on a positively-charged amine-modified surface to further understand substrate-influence on protein surface coverage. Work presented herein shows that surface coverage of an adsorbed protein depends largely on the nature of the substrate and the protein structure | en_US |
dc.language.iso | en | en_US |
dc.publisher | University of Cape Coast | en_US |
dc.subject | Protein adsorption | en_US |
dc.subject | Fibrinogen | en_US |
dc.subject | Infrared reflection absorption spectroscopy | en_US |
dc.subject | Gold substrate21 | en_US |
dc.title | Investigation of adsorption characteristics of fibrinogen on modified gold substrates using infrared reflection absorption spectroscopy | en_US |
dc.type | Article | en_US |
Appears in Collections: | Department of Chemistry |
Files in This Item:
File | Description | Size | Format | |
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Investigation of Adsorption Characteristics of Fibrinogen.pdf | Article | 638.47 kB | Adobe PDF | View/Open |
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