Alexandria Digital Research Library

Computational studies of sequence-specific driving forces in peptide self-assembly

Author:
Jeon, Joohyun
Degree Supervisor:
M. Scott Shell
Place of Publication:
[Santa Barbara, Calif.]
Publisher:
University of California, Santa Barbara
Creation Date:
2014
Issued Date:
2014
Topics:
Chemistry, Polymer, Engineering, Materials Science, Engineering, Chemical, and Plastics Technology
Keywords:
Peptide self-assembly
Amyloids
Molecular dynamics
Diphenylalanine
Lattice model
Genres:
Online resources and Dissertations, Academic
Degree Grantor:
University of California, Santa Barbara. Chemical Engineering
Dissertation:
Ph.D.--University of California, Santa Barbara, 2014
Description:

Peptides are biopolymers made from various sequences of twenty different types of amino acids, connected by peptide bonds. There are practically an infinite number of possible sequences and tremendous possible combinations of peptide-peptide interactions. Recently, an increasing number of studies have shown a stark variety of peptide self-assembled nanomaterials whose detailed structures depend on their sequences and environmental factors; these have end uses in medical and bio-electronic applications, for example. To understand the underlying physics of complex peptide self-assembly processes and to delineate sequence specific effects, in this study, I use various simulation tools spanning all-atom molecular dynamics to simple lattice models and quantify the balance of interactions in the peptide self-assembly processes. In contrast to the existing view that peptides' aggregation propensities are proportional to the net sequence hydrophobicity and inversely proportional to the net charge, I show the more nuanced effects of electrostatic interactions, including the cooperative effects between hydrophobic and electrostatic interactions. Notably, I suggest rather unexpected, yet important roles of entropies in the small scale oligomerization processes. Overall, this study broadens our understanding of the role of thermodynamic driving forces in peptide self-assembly.

Physical Description:
1 online resource (148 pages)
Format:
Text
Collection(s):
UCSB electronic theses and dissertations
ARK:
ark:/48907/f3rv0kvg
ISBN:
9781321567991
Catalog System Number:
990045118410203776
Rights:
Inc.icon only.dark In Copyright
Copyright Holder:
Joohyun Jeon
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