Interaction Studies of antimicrobial peptides with bacterial proteins by NMR

Description

The steadily increasing problem of bacterial resistance to common antibiotics intensifies the search for alternative ways to control resistant pathogens, causing thousands of deaths each year. A promising way to overcome this rising imminence is the use of antimicrobial peptides (AMPs) as leads. ORFormer [1] AMPs are especially useful because of their property to selectively inhibit metabolic pathways crucial for reproduction and metabolic survival of pathogens. [2] The study aims for inhibition of essential synthetic pathways of gram positive bacteria, which should be achieved by interfering the interaction of the acyl carrier protein with an artificial peptide. In the context of the study several de novo designed AMPs were investigated for their secondary structure propensities, wherefore tailored sets of 2D NMR exper- iments suitable for unlabelled peptides were used. From the obtained resonance assignments and NMR parameters, applied to algorithmic methods and used for comparison to database structures the observation of altered conformations upon post-translational added tags was made. Additionally to the mentioned methods, the relaxation rate in the rotating frame (t1rho) was determined by manipulation of a common TOCSY sequence. To study the binding process of the peptide to the protein, group-selective saturation transfer difference (STD) NMR spectroscopy as well as transferred NOE experiments are applied. [3-5]

Period	28 Mar 2018
Event title	BISSL (Bilateral Impromptu Symposium (Stockholm-Linz) on NMR Spectroscopy
Event type	Conference
Location	AustriaShow on map