Investigation of biorecognition process using force spectroscopy, AFM with molecular functionalized tip
Date of Issue2017-11-23
School of Materials Science and Engineering
Biorecognition process is the core of all biological interactions including interaction of cells, lipids, proteins and DNA. These Adhesion events in chemistry and biology are characterized by intermolecular interactions between particular chemical functionalities with noncovalent bonds, such as van der Waals, ionic or hydrophobic interactions. Furthermore, shape complementarities play a crucial role in the molecular recognition or biorecognition. Force spectroscopy measurement is one of the promising and versatile tool for the quantitative characterization of these binding forces and molecular interactions. On the basis of atomic force microscopy (AFM), force spectroscopy uses the tip functionalization as a means of evaluating binding specificity into interaction measurements. In practice, a chemically functionalized AFM tip is brought into contact with also chemically modified substrate with specific functionality and as the tip is retracted, the binding force between the two target molecular pair is measured. In this dissertation, we investigated the biorecognition process with biomaterials using force spectroscopy, AFM. The determination of the binding interactions which can control the biological functions will be described, focusing particularly peptide-inorganic materials and peptide-cellular membrane components. Based on the previous force spectroscopy measurement, the investigation of biomolecular interaction with various experimental factors will be proposed. A force-distance curve, the main output of force spectroscopy measurement, contains a lot of information to determine the mechanical properties of samples. To extract dependable and reproducible information, there are several experimental parameters and statistical analysis which should be contemplated. Estimating the binding mechanism which governs molecular complexes and understanding the strength of biomolecular associations lead to a fundamental knowledge of how the specific peptide interacts to biomaterials and consequently elucidate the biorecognition system and applications.