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Creation of Peptide-based Oligomers and Tailored Surfaces as Piezoelectric Biomaterials

Grimm, Haley, M. (2020) Creation of Peptide-based Oligomers and Tailored Surfaces as Piezoelectric Biomaterials. Doctoral Dissertation, University of Pittsburgh. (Unpublished)

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Peptides and proteins are advantageous as biomaterials due to their biocompatibility and flexible nature. A growing understanding of sequence/structure relationships and the conception of unnatural foldamers, scaffolds that can mimic folds similar to those found in nature, has opened doors to new architectures and materials properties. These scaffolds have shown promise as biosensors and bioelectronics. Hindering such work, however, is the fact that the surface environment can have profound effects on the predictability of folding behavior. This can result in a loss of stability or activity when a sequence of interest is tethered to an inorganic substrate. This dissertation details my work towards understanding how biomolecule folding is affected by surface properties and how molecular and surface properties combine to affect the inherent electromechanical nature of peptides and foldamers.
Chapter 2 explores the molecular origins of the piezoelectric response (the mechanical deformation arising from an electrical input) of peptide and peptoid self-assembled monolayers (SAMs). A series of designed molecules, where side chain and backbone composition was varied to alter the folding propensity, was used to test the hypothesis that backbone conformation influences electromechanical response. The piezo response of polar monolayers arising from the self-assembly of these molecules on a substrate was quantified by piezoelectric force microscopy. I conclude that backbone rigidity is an important determinant in peptide electromechanical response.
Chapter 3 aims to expand our understanding of the influence surface attachment has on peptide and protein conformation. A series of synthetic peptides were incorporated onto tailored-composition alkanethiol SAMs on gold surfaces via copper-catalyzed azide alkyne cycloaddition. The resulting surfaces were examined via polarization modulated infrared reflection absorption spectroscopy (PM-IRRAS) to assess peptide conformational preferences in response to changing surface properties. While surface density and polarity did not significantly alter peptide conformation for these systems, a more complex system, the bacterial alkaline phosphatase (BAP) enzyme, was affected. Upon incorporation onto our synthetic surfaces, the enzymatic activity of BAP was influenced by the surface context, showing a sharp decrease in activity when attached to a hydrophobic substrate.


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Item Type: University of Pittsburgh ETD
Status: Unpublished
CreatorsEmailPitt UsernameORCID
Grimm, Haley, M.hmg34@pitt.eduhmg34
ETD Committee:
TitleMemberEmail AddressPitt UsernameORCID
Committee ChairHorne, W.
Committee MemberHutchison, Geoffrey,
Committee MemberFloreancig,
Committee MemberAshkenasy,
Date: 16 January 2020
Date Type: Publication
Defense Date: 26 September 2019
Approval Date: 16 January 2020
Submission Date: 1 December 2019
Access Restriction: No restriction; Release the ETD for access worldwide immediately.
Number of Pages: 188
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: Biomaterials, piezoelectrics, surface chemistry, self-assembled monolayers, peptides
Date Deposited: 16 Jan 2020 18:38
Last Modified: 16 Jan 2020 18:38

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