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Kinetic Analysis of the Effect of Crowding on AgNP Surface Bound NHS Ester Reactions with Imidazole

Persistent URL
https://dspace.allegheny.edu/handle/10456/56801
Author(s)
Nese, William
Date Issued
April 13, 2023
Abstract
The attachment of proteins as recognition systems is important for both the function and the design of most biosensors. However, crowding of molecules at the surface can often affect surface reactions such as these. Thus, the goal was to understand how surface crowding affects the speed and extent of reactions commonly used to tether proteins to a surface by adding various ratios of 4-mercaptobenzoic acid (4-MBA) and thiophenol on surfaces. The kinetics of the reaction between solution-phase imidazole and a surface bound N-hydroxysuccinimide (NHS) ester of 4-MBA has been investigated using surface-enhanced Raman scattering. The rate constant and extent of reaction were monitored. The surface reactions were found to go nearly to completion with an average second order rate constant of 0.005 mM-1s-1, yet no clear relationship between surface crowding and percent conversion from NHS ester to imidazole was determined.
Major
Chemistry
First Reader(s)
Deckert, Alice A.
Other Reader(s)
Guldan, Beth
Ams, Mark R.
Department
Chemistry
Type of Publication
Senior Project Paper
Subjects

kinetic analysis

crowding

AgNP surface

NHS ester

imidazole

recognition systems

tether attachment

File(s)
Thumbnail Image
Name

Nese_Thesis.docx.pdf

Size

1.29 MB

Format

Adobe PDF

Checksum (MD5)

9d4a7310e44dbc34df52ed18c97396ef

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