"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.
Al-Dahhan, Muthanna H.
Neogi, P. (Partho), 1951-
Chemical and Biochemical Engineering
M.S. in Chemical Engineering
National Science Foundation (U.S.)
Missouri University of Science and Technology
ix, 70 pages
© 2012 Kunal Mukesh Naik, All rights reserved.
Thesis - Open Access
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Link to Catalog Recordhttp://laurel.lso.missouri.edu/record=b9390258~S5
Naik, Kunal Mukesh, "Formation of amyloid fibrils by diblock peptides" (2012). Masters Theses. 5137.