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SUMMARY:Discovering peptide inhibitors against FtsY\, an antibiotic target
DTSTART;VALUE=DATE-TIME:20211125T065500Z
DTEND;VALUE=DATE-TIME:20211125T065600Z
DTSTAMP;VALUE=DATE-TIME:20260310T132717Z
UID:indico-contribution-4204@events01.synchrotron.org.au
DESCRIPTION:Speakers: Jennifer Zhao (University of Sydney)\nThe rapid rise
  of antibiotic resistance has caused an urgent demand for new antibiotics.
  One way to address this is by manipulating essential bacterial interactio
 ns not targeted by current antibiotics. The interaction between the Signal
  Recognition Particle (SRP) and its receptor (FtsY) is critical for cell v
 iability but is mediated by RNA:protein interactions in bacteria versus pr
 otein:protein interactions in eukaryotes. We have used a new technology kn
 own as RaPID (Randomised non-standard Peptide Integrated Discovery) to ide
 ntify cyclic peptides that bind to FtsY. Sequence enrichment was observed 
 after seven rounds of selection and eight representative peptides were sel
 ected for further characterisation.\n \nTo determine whether the peptides 
 can bind the intended RNA-binding interface on FtsY\, Nuclear Magnetic Res
 onance Spectroscopy (NMR) spectra were collected on 2H13C15N-FtsY produced
  by ANSTO. High deuteration level has facilitated good quality NMR spectra
  despite the large size of FtsY (35 kDa). In total\, ~220 amide groups wer
 e mapped onto the “fingerprint” 15N-1H-HSQC spectrum with >75% of back
 bone resonances assigned. Following peptide synthesis\, we will titrate se
 lected peptides into labelled FtsY for chemical shift perturbation experim
 ents. This will provide binding affinity data for the different peptides a
 nd enable the mapping of binding residues onto our previously solved cryst
 al structure. The highest affinity binders will be subjected to soaking an
 d co-crystallisation experiments with FtsY to further characterise the mod
 e of interaction. Taken together\, the data obtained will inform the futur
 e development of cyclic peptides into FtsY inhibitors with high affinity a
 nd specificity as potential antibiotic leads.\n\nhttps://events01.synchrot
 ron.org.au/event/146/contributions/4204/
LOCATION:Online
URL:https://events01.synchrotron.org.au/event/146/contributions/4204/
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