Publication Date

2014-12-17

Availability

Open access

Embargo Period

2014-12-17

Degree Type

Dissertation

Degree Name

Doctor of Philosophy (PHD)

Department

Chemistry (Arts and Sciences)

Date of Defense

2015-08-18

First Committee Member

Roger Leblanc

Second Committee Member

Carl Hoff

Third Committee Member

James Wilson

Abstract

The focus of this thesis can be categorized as study of two molecules, namely human insulin and carbon dots at 1) air-water interface as a Langmuir monolayer and 2) in solution. Aggregation of proteins into amyloids has been related to several diseases like Alzheimer’s, Parkinson’s and Amyloidosis. Human insulin was chosen as a model protein to study fibrillation of the proteins. Effect of carbon dots on the rate of human insulin fibrillation was examined through spectroscopic techniques and imaging. Both human insulin and carbon dots were examined at air-water interface as a Langmuir monolayer. The conformation of human insulin in presence of various salt concentration and ZnCl2 was examined at air-water interface. Based on the results of the surface pressure isotherms and spectroscopic studies of the protein at air-water interface, an scheme was proposed for the conformation of human insulin at air-water interface. Carbon dots at air-water interface were imaged by Atomic Force Microscopy using Langmuir-Blodgett films.

Keywords

Langnuir monolayer, surface chemistry, insulin, nanocrystals, air-water interface,

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