Synthesis of anthracene-conjugates of truncated antifreeze protein sequences. Effect of end-group and photo-controlled dimerization on ice recrystallisation inhibition activity.

Synthesis of anthracene-conjugates of truncated antifreeze protein sequences. Effect of end-group and photo-controlled dimerization on ice recrystallisation inhibition activity. Biomacromolecules. 2019 Nov 12;: Authors: Graham B, Fayter AER, Gibson MI Abstract Biomacromolecular antifreezes distinguish ice from water, function by binding to specific planes of ice and could have many applications from cryobiology to aerospace where ice is a problem. In biology, antifreeze protein (AFP) activity is regulated by protein expression levels via temperature and light regulated expression systems but in the laboratory (or applications) the antifreeze activity is 'always on' without any spatial nor temporal control and hence methods to enable this switching represent an exciting synthetic challenge. Introduction of abiotic functionality into short peptides (e.g. from solid phase synthesis) to enable switching is also desirable, rather than on full-length recombinant proteins. Here truncated peptide sequences based on the consensus repeat sequence from Type I AFPs (TAANAAAAAAA) were conjugated to an anthracene unit to explore their photo-controlled dimerization. Optimization of the synthesis to ensure solubility of the hydrophobic peptide included the addition of a dilysine solubilizing linker. It was shown that UV-light exposure triggered reversible dimerization of the AFP sequence, leading to an increase in molecular weight. Assessment of the...
Source: Biomacromolecules - Category: Biochemistry Authors: Tags: Biomacromolecules Source Type: research