DNA Mimic Foldamer Recognition of a Chromosomal Protein

03 November 2023, Version 1
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

Helical aromatic oligoamide foldamers bearing anionic side chains that mimic the overall shape and charge surface distribution of DNA were synthesized. Their interactions with chromosomal protein Sac7d, a non-sequence-selective DNA-binder that kinks and packages DNA, were investigated by Surface Plasmon Resonance (SPR), Circular Dichroism (CD), and Nuclear Magnetic Resonance (NMR) spectroscopies, as well as by single crystal X-ray crystallography. The foldamers were shown to bind to Sac7d better than a DNA duplex of comparable length. The interaction is diastereoselective and takes place at the DNA-binding site. Crystallography revealed that the DNA-mimic foldamers have a binding mode of their own and that they can bind to Sac7d without being kinked.

Keywords

Chromosomal Proteins
DNA Mimicry
Foldamers
Protein Recognition
Structure Elucidation

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