Poster abstracts

Poster number 16 submitted by Danielle Dremann

Peptide binding studies with helix 69 of the bacterial ribosome

Danielle N. Dremann (Chemistry, Wayne State University), Moninderpal Kaur (Chemistry, Wayne State University), Christine S. Chow (Chemistry, Wayne State University)

Abstract:
Helix 69 (H69) is located within the large subunit of the bacterial ribosome and has been implicated to have a role in protein synthesis. Previously, the phage display technique provided the peptide sequence NQVANHQ, which was shown to bind to H69 with moderate binding affinity. In this study, modifications of this peptide were produced using solid-phase synthetic approaches. This technique offers an efficient way of synthesizing heptamers with various modifications. Fourteen peptides were synthesized for the initial stage of this project. Binding studies using the electrospray ionization mass spectrometry (ESI-MS) technique yielded a dissociation constant for each peptide – RNA complex. These studies provide information regarding which functional groups on the peptide are necessary for binding to H69. Using ESI-MS, competition reactions between modified peptides and the parent sequence NQVANHQ were performed to further study binding efficiency. A combination of these peptide modifications could provide an optimized binder with greater binding affinity to the target RNA which can be further tested to identify potent inhibitors of protein synthesis of the bacterial ribosome.

Keywords: peptide, helix 69, ribosome