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Phage display screening in low dielectric media
Linus Olofsson1, Pernilla Söderberg, Jonas Ankarloo
1Bioorganic and Biophysical Chemistry Laboratory, School of Pure and Applied Natural Sciences, University of Kalmar, Kalmar, Sweden.
Journal of Molecular Recognition : JMR
|July 26, 2008
Summary
Phage display screening was applied in low dielectric media for the first time. This method successfully identified peptides that protect alpha-chymotrypsin (CT) from degradation, enhancing its activity in non-aqueous environments.
Area of Science:
- Biotechnology
- Biochemistry
- Enzyme kinetics
Background:
- Phage display is a powerful technique for selecting peptides with specific binding properties.
- Low dielectric media, such as acetonitrile, present challenges for biological assays due to their potential to denature proteins.
- Alpha-chymotrypsin (CT) is a serine protease sensitive to its environment.
Purpose of the Study:
- To investigate the feasibility of applying phage display screening in low dielectric media.
- To identify peptides that can stabilize alpha-chymotrypsin (CT) in acetonitrile-containing solutions.
- To evaluate the impact of screening conditions on peptide selection and enzyme activity.
Main Methods:
- Selection of phage clones from a Ph.D.(TM)-C7C library against CT in two conditions: standard buffer and 50% acetonitrile in buffer.
- Affinity assessment of selected phage lysates, individual clones, and cyclic peptides by measuring their effect on CT activity.
- Analysis of enzyme autolysis and protection from acetonitrile-induced detrimental effects.
Main Results:
- Phage clones selected in buffer yielded peptides that significantly increased CT activity (>100%) by protecting it from autolysis.
- Phage clones selected in 50% acetonitrile showed a weaker, but noticeable, protective effect against acetonitrile's detrimental impact on CT.
- The study demonstrated successful peptide selection in a low dielectric medium.
Conclusions:
- Phage display screening is applicable to targets in low dielectric media.
- Peptides selected in non-aqueous environments can confer stability and activity to enzymes.
- This approach opens new possibilities for enzyme stabilization and engineering in non-traditional solvents.
