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Identifier

000402455

Title

Study of self-assembling peptides that contain aromatic amino acids

Alternative Title

Μελέτη αυτοοργάνωσης πεπτιδίων τα οποία περιέχουν αρωματικά αμινοξέα

Author

Ορνιθοπούλου, Ειρήνη

Thesis advisor

Μητράκη, Άννα

Reviewer

Βαμβακάκη, Μαρία
Πετράτος, Κυριάκος

Abstract

Peptides are promising building blocks for tissue engineering applications. In the current thesis, an amyloidogenic peptide sequence –inspired by the Adenovirus fiber shaft- is rationally designed to carry photo-structuring and cell-adhesive components. For photo-structuring, aromatic amino acids that have been grafted on to the N- or C- terminus are: Tyrosine, Tryptophan, Phenylalanine and Histidine. For cell adhesion the RGD tripeptide has been positioned on the N terminus. The RGD is known to mimic Fibronectin’s activity in the Extracellular Matrix as a cell adhesion agent. Electron Microscopy, Atomic Force Microscopy, X-ray Fiber Diffraction and Congo red staining were used to establish the structure of the produced gels, which definitely showed the unaffected ability of these designed peptides to build amyloid fibrous networks. For Photo structuring a KrF pulsed laser has been used, along with the Laser-Induced Fluorescence technique to examine the production of photo-oxidized moieties, and possible crosslinks. Preliminary results, using mouse 3T3 fibroblasts show a preference of the cells to adhere and proliferate on the irradiated surface; therefore, these materials can be candidates for tissue engineering applications. Finally, an RGD- and Histidine containing peptide is shown to reduce its gelation time exponentially when treated with ultrasound.

Language

English, Greek

Subject

Tissue engineering

Ιστοτεχνολογία

Issue date

2016-07-22

Collection

School/Department--School of Sciences and Engineering--Department of Materials Science and Technology--Post-graduate theses

Type of Work--Post-graduate theses

Permanent Link

https://elocus.lib.uoc.gr//dlib/6/3/9/metadata-dlib-1469608003-537000-20657.tkl