Biofunctional Nanofibers and Supramolecular Hydrogels of Naphthalimide-based Peptides

碩士 === 國立交通大學 === 材料科學與工程學系所 === 103 === Adhesive peptide sequences within many ECM proteins have been discovered via competitive adhesion assays and mutagenesis experiment. In our laboratory, Novel hydrogels based on Naphthalimide with peptide sequences DGEA, IKVAV, GFF, and FFG have been synthesiz...

Full description

Bibliographic Details
Main Authors: Huang, Ching-Ting, 黃敬婷
Other Authors: 林欣杰
Format: Others
Language:en_US
Published: 2014
Online Access:http://ndltd.ncl.edu.tw/handle/jqjq6a
Description
Summary:碩士 === 國立交通大學 === 材料科學與工程學系所 === 103 === Adhesive peptide sequences within many ECM proteins have been discovered via competitive adhesion assays and mutagenesis experiment. In our laboratory, Novel hydrogels based on Naphthalimide with peptide sequences DGEA, IKVAV, GFF, and FFG have been synthesized. This thesis has three-fold. In the first part, DGEA-containing peptides hydrogelators based on naphthalimide are developed. The DGEA tetra-peptide sequence is the shortest collagen type I-derived motif recognized by the collagen-binding integrin 21. Also, the materials have significant differences in their fluorescence intensity because of the capping group, 1,8-Naphthalimide-N-acetic acid and 4-Nitro-1,8-Naphthalimide-N-acetic acid. In the second part, small molecule hydrogels containing IKVAV polypeptide induced self-assembly to form nanofiber gel was synthesized. The IKVAV peptide sequence is located in the α-1 chain of laminin responsible for cell adhesion and neurite outgrowth. We reduce the molecular weight of IKVAV-containing hydrogelator and toward a better material that fits the Atomic economy and Green chemistry. In the last one, we capped peptide sequences, GFF and FFG with aromatic group, naphthalimide, and compared the cell viability of NI-GFF and NI-FFG. We also tested the cell viability of 4-Nitro-1,8-naphthalimide, NO2-FDGEA and NO2-FIKVAV to know whether if the cytotoxicity of the materials can be improved by conjugating the peptide sequences.