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Mustafa O. Guler

Researcher at University of Chicago

Publications -  189
Citations -  7106

Mustafa O. Guler is an academic researcher from University of Chicago. The author has contributed to research in topics: Peptide amphiphile & Nanofiber. The author has an hindex of 42, co-authored 183 publications receiving 6188 citations. Previous affiliations of Mustafa O. Guler include Northwestern University & Bilkent University.

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Intermolecular forces in the self-assembly of peptide amphiphile nanofibers

TL;DR: In this paper, the authors used oscillatory rheology, Fourier transform infrared spectroscopy, and circular-dichroism spectrograms to understand the assembly mechanism of a typical PE molecule known as PA-1, which is triggered by counterion screening and stabilized by van der Waals and hydrophobic forces.
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Self-assembled peptide amphiphile nanofibers conjugated to MRI contrast agents.

TL;DR: The synthesis of magnetic resonance (MR) active peptide amphiphile molecules that self-assemble into spherical and fiber-like nanostructures, enhancing T(1) relaxation time is reported, which can potentially be used to combine high-resolution three-dimensional MR fate mapping of tissue-engineered scaffolds with targeting of specific cellular receptors.
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Hybrid bone implants: self-assembly of peptide amphiphile nanofibers within porous titanium.

TL;DR: A method to prepare a hybrid bone implant material consisting of a Ti-6Al-4V foam, whose 52% porosity is filled with a peptide amphiphile (PA) nanofiber matrix, to improve fixation, osteointegration, and long term stability of implants is reported on.
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A self-assembled nanofiber catalyst for ester hydrolysis

TL;DR: In this paper, a self-assembling peptide amphiphiles (PAs) were synthesized in order to form high-aspect-ratio nanofibers with internal order that can present imidazolyl groups capable of ester hydrolysis.
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Supramolecular crafting of cell adhesion

TL;DR: Self-assembling supramolecular nanofibers that display the cell adhesion ligand RGDS at van der Waals density to cells are used and it is found that branched architectures of the monomers and the consequent lower packing efficiency and additional space for epitope motion improves signaling forcell adhesion, spreading, and migration.