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Effects of Peptide Sequence in Controlling the Assembly Propensity and Structural Morphology of Helical Gold Nanoparticle Superstructures

Brooks, Sydney (2023) Effects of Peptide Sequence in Controlling the Assembly Propensity and Structural Morphology of Helical Gold Nanoparticle Superstructures. Doctoral Dissertation, University of Pittsburgh. (Unpublished)

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Peptide-based materials incorporate the hierarchical structure of proteins: amino acids on the molecular scale dictate the secondary structure, which in turn affects the overall protein folding and function. Similarly, peptides and proteins can promote the growth of inorganic minerals with extreme precision, creating the composite substances that make up skeletons, shells, and other hard biological materials. The ability to synthetically harness this capability and use it to make equally precise materials in a laboratory could lead to the synthesis of new materials with applications in optics, sensing, and nanotechnology. By studying biomineralization, scientists have learned some of the design rules to synthesizing functional hybrid nanomaterials. The Rosi group has spent over a decade developing a peptide-based assembly system for inorganic nanoparticles (NPs). Starting with a peptide amphiphile designed to bind gold nanoparticles (Au NP) and assemble into fibers, we have developed a suite of design rules to synthesize a variety of nanostructures as well as dictate their structural morphology and function. This dissertation describes several research projects aimed at understanding the effect of molecular changes to the peptide conjugate within an Au NP assembly system and leveraging them as tunable handles that we can use to control structural parameters of the resultant Au NP superstructures. In Chapter 1, a general discussion of peptide amphiphiles and peptide biomineralization is followed by an introduction of the group’s work on nanoparticle assembly. In Chapter 2, the assembly module (organic tail and peptide N-terminal amino acids) of the peptide conjugate was examined, and a method to tune fiber and Au NP assembly propensity by increasing the -sheet contribution of the peptide sequence was developed. In Chapter 3, the role of the particle binding module (C-terminal amino acids) in superstructural differentiation is investigated. By introducing a series of modifications with decreasing Au-binding affinity, it was determined that Au NP-peptide contact dictated the structure from aggregates (high) to single helices (moderate) to discrete Au NPs (low). Finally, I investigated the effect of electrostatic contributions to the particle binding module, and explore cooperative peptide conjugate assembly by leveraging attractive interactions in Chapter 4.


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Item Type: University of Pittsburgh ETD
Status: Unpublished
CreatorsEmailPitt UsernameORCID
Brooks, Sydneyscb87@pitt.eduscb87
ETD Committee:
TitleMemberEmail AddressPitt UsernameORCID
Committee ChairRosi, Nnrosi@pitt.edunrosi
Committee MemberLaaser, Jj.laaser@pitt.eduj.laaser
Committee MemberMillstone, Jjem210@pitt.edujem210
Committee MemberBanerjee, Iipb1@pitt.eduipb1
Date: 11 May 2023
Date Type: Publication
Defense Date: 2 March 2023
Approval Date: 11 May 2023
Submission Date: 7 April 2023
Access Restriction: No restriction; Release the ETD for access worldwide immediately.
Number of Pages: 181
Institution: University of Pittsburgh
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Degree: PhD - Doctor of Philosophy
Thesis Type: Doctoral Dissertation
Refereed: Yes
Uncontrolled Keywords: peptide synthesis, peptide assembly, chiral nanoparticle superstructures, plasmonic nanoparticles
Date Deposited: 11 May 2023 14:32
Last Modified: 11 May 2023 14:32


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