Selective fluorescence sensing of biological thiols using a bodipy based bifunctional probe and the catalytic activity of short peptide amphiphile nanostructures : implications on the oring of life
Author(s)
Advisor
Akkaya, Engin U.Date
2013Publisher
Bilkent University
Language
English
Type
ThesisItem Usage Stats
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Abstract
Chemosensor development is an attractive field of modern chemistry and there exist
large amount of contribution from all over the world. The biological importance of
thiols triggered the development of sensors to differentiate especially cysteine (Cys),
homocysteine (Hcy) and glutathione (GSH) which play key roles in biological
systems. Concentration of those thiols results in number of diseases and their
structural similarity complicates the differentiation. Optical probes especially
fluorescent ones are widely employed for that purpose since it offers simplicity,
sensitivity and low detection limits as well as real time analysis. BODIPY core is
decorated with a Michael acceptor nitro-styrene group to covalent incorporation of
thiols and with an aza-crown moiety to recognition of N-terminus of them. The work
in this thesis is the first example in which one of them is separated from others or
three of them separated from each other’s by chain length difference using
fluorescence spectrometry.
Formation of short peptides (2-4 aa residues) is considered to be likely under
primordial conditions, following a number of scenarios. In this work, it is
constructed a short peptide library limiting our choice of amino acids to those
believed to be available at larger concentrations such as Gly, Ala, Asp and Cys. It is
demonstrated that when acylated at the N-terminus, nanostructures of varying size
and shapes were formed. Investigations on the catalytic activity of these
nanostructures under different conditions are presented. The findings on the
correlation of peptide structure and nanostructure formation and/or catalytic activity
are presented.