Photophysical Approach to Study the Interaction Between Synthetic Amphiphiles and Proteins
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2011
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Abstract
The contents of the thesis entitled “Photophysical Approach to Study the Interaction between Synthetic Amphiphiles and Proteins” have been divided into five chapters based on the results of experimental works carried out during the research period. Chapter 1 highlights the definition, properties and importance of synthetic amphiphiles along with their literature background. Amphiphilic molecules consist of hydrophobic tail (usually made of long hydrocarbon chains) and hydrophilic head group (either charged or uncharged polar groups). As a result of having both hydrophobic and hydrophilic structural regions, amphiphilic molecules may dissolve in water and to some extent in non-polar organic solvents. This chapter also gives a brief overview of interaction between synthetic amphiphiles and biomolecules especially protein, where nature of head group and hydrophobic tail along with electrostatic and hydrogen bonding interactions play crucial role. Many amphiphilic molecules are known to interact with peptides and proteins, being that these interactions are of great importance not only in vivo but also in several technical applications. This forms the basis of a number of research areas in chemistry, biochemistry and materials science as well. Therefore, study of interaction between synthetic amphiphiles and proteins and the structure of the complexes formed as a result of those interactions have been extensively reviewed in this chapter. Chapter 2 deals with the common methodology used to synthesize and characterize the compounds along with a brief description of equipments and the different experimental setup to study the interactions between amphiphiles and proteins. Chapter 3 describes the interaction between 5-(alkoxy)naphthalen-1-amine (1-3) amphiphile and bovine serum albumin (BSA). The content of this chapter is divided into two sections. The first section reports the selective sensing of BSA by these novel protein binding amphiphilic fluorophores (1-3) via. non-covalent interactions. The weak fluorescent of these probes in an aqueous solution showed a dramatic increase in their fluorescence intensity, quantum yield and lifetime after binding with BSA (Fig. 1). The exclusivity of the system is that it interacts with BSA selectively and signals the event by ‘turn on” fluorescence while the responses to various other proteins/enzymes used are negligible under similar set of experimental conditions. The photophysical behaviour of compounds are affected by the interplay with BSA but not with free tryptophan amino acid suggesting the microenvironment created by macromolecule induces some change in the excited-state of compound....
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Supervisor: Gopal Das
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CHEMISTRY