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The design, characterization and utility of self-assembling hydrophobic collagen peptides
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McGuinness, Kenneth N.. The design, characterization and utility of self-assembling hydrophobic collagen peptides. Retrieved from https://doi.org/doi:10.7282/T3K076B0

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TitleThe design, characterization and utility of self-assembling hydrophobic collagen peptides
NameMcGuinness, Kenneth N. (author); Nanda, Vikas (chair); Shreiber, David (internal member); Dutt, Meenakshi (internal member); Stock, Ann (internal member); Murthy, Sanjeeva (outside member); Rutgers University; Graduate School - New Brunswick
Date Created2016
Other Date2016-01 (degree)
SubjectComputer Science, Self-assembly (Chemistry), Collagen, Peptides
Extent1 online resource (xiii, 80 p. : ill.)
DescriptionThis thesis will focus on predicting and characterizing the self-assembly of collagen mimetic peptides and their interactions with natural proteins with varying secondary structure and exposed surface hydrophobicity. Chapter 1 will provide an overview of the forces that affect peptide self-assembly, and describe why the collagen triple-helix is a good model system for studying self-assembly. In Chapter 1, a set of synthetic collagen peptides, that were designed using diffusion limited aggregation (DLA) simulations, are used to probe the role of hydrophobic forces that govern protein self-assembly. DLA simulations predicted that length and pattern of the hydrophobic domain is an important driver of morphology. In Chapter 1, length of hydrophobic sequence is shown to be potentially more important in directing peptide self-assembly. Sequences with four, five and six consecutive hydrophobic residues results in the formation of discs, discs and fibers, and all fibers, respectively. In Chapter 2, the discs formed in Chapter 1 are used to probe the nature of protein-protein interactions. The utilization of peptide nanostructures as scaffolds and substrates for creating new materials and understanding the surface properties of existing proteins is explored. Mixtures of peptide nanostructures and natural proteins provide evidence that peptide nanostructures can be used as membrane surrogates for membrane proteins, sites of nucleation for fiber assembly, and as a probe for surface hydrophobicity. Chapter 2 highlights that hydrophobicity can potentially be used to target protein structures generally, e.g. alpha helices and beta sheets. Appendix 1 takes a closer look into the morphology of H4 discs in solution. Appendix 2 sheds light on the interactions between molecules with the same and opposite chirality. This study utilizes the ‘chemically nude’ (PPG)10 triple-helix to show that self-assembly into nanostructures is geometrically favorable only between opposite-handed triple helices. The implications of favorable packing preference between opposite-handed helices will be discussed.
NotePh.D.
NoteIncludes bibliographical references
Noteby Kenneth N. McGuinness
Genretheses, ETD doctoral
Persistent URLhttps://doi.org/doi:10.7282/T3K076B0
Languageeng
CollectionGraduate School - New Brunswick Electronic Theses and Dissertations
Organization NameRutgers, The State University of New Jersey
RightsThe author owns the copyright to this work.
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