Self-assemblies of electrostatically self-complementary peptides derived from different structural motifs Restricted; Files & ToC

Abstract

Supramolecular self-assembly from peptides is a powerful bottom-up approach for the fabrication of bio-nanomaterials. Peptides are advantageous among the sequence-programmable oligomers because of their sequence-specificity and chemical diversity, hence offering a great opportunity to introduce functional complexity across length-scales. However, it is currently still challenging to achieve controlled fabrication of structurally and dimensionally defined assemblies. This dissertation presents our effort in the fabrication of one- and two-dimensional nanomaterials from the self-assemblies of peptide sequences that are electrostatically self-complementary. The general construct of the peptides consists of two end blocks with oppositely charged residues and a midblock that is neutral. The peptide sequences are designed based on two structural motifs, collagen triple helices and -sheets. The collagen-mimetic peptides (CMPs) fold into triple helices, which subsequently self-assemble into two-dimensional crystalline nanosheets via electrostatic interaction. In this work, we utilize CMPs for the construction of multicomponent nanosheets with tunable properties. Even though our study of the -strand mimetic peptides (BMPs) is still at its infancy, preliminary results indicate that the charge-complementary sequence design in combination with D-amino acid substitution promote very robust growth of BMPs into one-dimensional nanotubes. Our current findings suggest that the relatively simple design of electrostatically self-complementary peptides works across multiple structural motifs and may present a promising strategy for controlled fabrication of peptide-based nanomaterials.

Table of Contents

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About this Dissertation

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School	Laney Graduate School
Department	Chemistry
Degree	Ph.D.
Submission	Dissertation
Language	English
Research Field	Biophysics, Biomechanics Chemistry, General Chemistry, Biochemistry
Keyword	Peptide self-assembly Bionanomaterials
Committee Chair / Thesis Advisor	Vincent Conticello, Emory University
Committee Members	Yonggang Ke, Emory University David Lynn, Emory University

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