Masters Theses

Abstract

"The objective of this study was to identify and then synthesize a series of peptides which were able to form fibrils rich in ß-sheet structure and to study the effect of the presence of surfaces on their formation. We decided to focus our experimental work on a family of peptides containing one "beta-sheet forming amino acid" and one 'alpha-helix forming amino acid'. This selection covers a wide range of hydrophillicites and charges and, by avoiding highly hydrophobic amino acids we can assure that the diblock peptides are soluble in a wide range of concentrations and solvent conditions. Three different diblocks (20:80; 50:50 and 80:20) were synthesized. The aggregation studies were done in the absence and in the presence of solid/liquid interfaces. Two types of surfaces were used: polystyrene latexes with different surface chemistry and liposomes. The rate and extent of aggregation was followed by dynamic light scattering, which was used to monitor the size of the aggregates as a function of time. Congo Red assays were performed to confirm if the aggregates were amyloidic and selected samples were inspected by optical, scanning and atomic force microscopy. Secondary structure of the fibrils was studied using FT-IR"--Abstract, page iii.

Advisor(s)

Forciniti, Daniel

Committee Member(s)

Al-Dahhan, Muthanna H.
Neogi, P. (Partho), 1951-

Department(s)

Chemical and Biochemical Engineering

Degree Name

M.S. in Chemical Engineering

Sponsor(s)

National Science Foundation (U.S.)

Publisher

Missouri University of Science and Technology

Publication Date

Spring 2012

Pagination

ix, 70 pages

Note about bibliography

Includes bibliographical references (leaves 65-67).

Rights

© 2012 Kunal Mukesh Naik, All rights reserved.

Document Type

Thesis - Open Access

File Type

text

Language

English

Library of Congress Subject Headings

Amyloid
Liposomes
Nanofibers
Peptides

Thesis Number

T 9975

Print OCLC #

815962349

Electronic OCLC #

776632171

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