Erkal, Turan Selman2016-01-082016-01-082012http://hdl.handle.net/11693/15509Ankara : The Materials Science and Nanotechnology Program of the Graduate School of Engineering and Science of Bilkent University, 2012.Thesis (Master's) -- Bilkent University, 2012.Includes bibliographical references leaves 80-82.Peptide nanofibers have been drawing attention because of their versatile, tailorable and functional properties in various research areas. The self-assembly mechanism of peptides and peptide amphiphile molecules is generally based on noncovalent interactions like hydrophobic, electrostatic and metal-ligand interactions. In this thesis, I investigated hydrophobic interaction of peptide amphiphiles (PAs) with other hydrophobic molecules and effect of pH change on self-assembly mechanism. The zinc phthalocyanine molecule was used as a hydrophobic probe to be encapsulated by peptide amphiphile molecules, which help to dissolve the molecule in water instead of an organic solvent. Charge neutralization of PAs by pH change led to nanofiber formation, which resulted in encapsulation and organization of zinc phthalocyanine molecules. The degree of self-assembly by pH change determined non-linear optical properties of zinc phthalocyanine molecule. Besides, morphological, mechanical and spectroscopic properties of phthalocyanine containing peptide nanofibers were characterized by TEM, SEM, oscillatory rheology, UV-Vis, fluorescence and circular dichroism spectroscopy. The mechanical properties of peptide and PA hydrogels and nanofibers have an essential place to determine applicability in different areas. Especially, PA and peptide molecules have been widely used in regenerative medicine studies and the stiffness of the extracellular matrix has a significant role on cellular behavior. In this thesis, viscoelastic properties of the peptide and PA gels were studied by oscillatory rheology. In addition to characterization of bulk mechanical properties of peptide gels, adhesion and stiffness of peptide nanofibers were determined by Atomic Force Microscopy.xiv, 82 leaves, illustrationsEnglishinfo:eu-repo/semantics/openAccessPeptide nanofiberself-assemblyencapsulationzinc phthalocyaninerheologyAtomic Force Microscopynanomechanical propertiesQP552.P4 E75 2012Peptides--Synthesis.Nanostructured materials.Thesis