4 research outputs found

    Investigating The Structural And Physiochemical Properties Of Collagen Mimetic Peptides With Modified Backbones

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    Collagen is the most abundant protein found in mammalian systems and is critically important in a myriad of different regulatory pathways, prompting widespread effort to model and understand collagen-protein interactions. A network of hydrogen bonds, non-covalent interactions, sterics, and stereoelectronic effects hold collagen’s unique triple-helical quaternary structure together. The highly repetitive primary structure, generalized by a three amino acid triplet: (Xaa-Yaa-Glycine), is critical for this uncommon structural assembly.Our lab has been investigating how the incorporation of aza-glycine (azGly, azG) and aza- proline (azPro, azP) residues affect the triple-helical structure and thermal stability of collagen mimetic peptides (CMPs). Although we have previously shown azGly and azPro incorporation can affect the triple-helical thermal stability of CMPs, the model systems used were quite limited in scope. Herein, the impact of azGly and azPro incorporation on CMP stability and structure is demonstrated to be dependent on a variety of different factors. This was accomplished through the synthesis of peptide libraries containing these aza-amino acids, evaluation of CMP thermal stabilities along with refolding times, and by solving high-resolution crystallographic structures of triple-helical structures. Futhermore, we optimize the synthesis of azGly-containing CMPs, evaluate the binding of azGly-containing CMPs to a target protein, and investigate an alternative CMP model system. Collectively, this body of work reports the first comprehensive set of design guidelines for incorporating azGly and azPro residues into CMPs and sets the stage for the utilization and application of aza-collagen peptides within biologically relevant systems

    Structural And Computational Insights In Collagen Stability With Applications In Light Harvesting

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    Collagen is the most abundant protein in mammals, constituting almost a third of the total protein content in the body. Its unique structure and versatility has attracted the attention of many researchers for the development of new types of materials. Here, the influence of the aza-amino acids α-azaproline, azaglycine, and -azaproline on the structure and stability of collagen is studied through incorporation into collagen model peptides (CMPs) and analyzed through a variety of computational methods including DFT and molecular dynamics calculations. Inspired by the success of generating multispectral imaging agents by using DNA as a scaffold for multichromophore assembly, the utilization of the distinctive self-assembly of collagen to template the arrangement of chromophores is also explored for the first time. Simple modifications regarding linker length, chromophore loading, chromophore spacing, and chromophore type are investigated and analyzed by computational methods to develop key insights in utilizing this novel scaffold for use in light harvesting applications. Separate projects regarding the development of novel photo-activatable probes based on the structure of xylopyridine, as well as chemical modifications to the pigment carbon black for the improvement of the jetness of coatings are also examined
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