Ribosome tolerates artificial foldamers


The mRNA-templated synthesis of peptides by the ribosome, can be manipulated to incorporate variants of the 20 cognate amino acids.

 Such approaches for expanding the range of chemical entities that can be produced by the ribosome may accelerate the discovery of molecules that can perform functions for which poorly folded, short peptidic sequences are ill suited.

Here, we show that the ribosome tolerates some artificial helical aromatic oligomers, so-called foldamers.

Using a flexible tRNA-acylation ribozyme—flexizyme—foldamers were attached to tRNA, and the resulting acylated tRNAs were delivered to the ribosome to initiate the synthesis of non-cyclic and cyclic foldamer–peptide hybrid molecules.

Make more money selling and advertising your products and services for free on Ominy market. Click here to start selling now

Passing through the ribosome exit tunnel requires the foldamers to unfold.

Yet foldamers encode sufficient folding information to influence the peptide structure once translation is completed.

We also show that in cyclic hybrids, the foldamer portion can fold into a helix and force the peptide segment to adopt a constrained and stretched conformation.
 Story source

READ MORE  Drinking baking soda could be an inexpensive, safe way to combat autoimmune disease

Ibezim chukwuemerie

EDM freak... Digital marketer... Tech savvy... In love with human science... Studies zoology at University of Nigeria... Chief editor at Ominy science. Follow him on Twitter and Instagram or like our page on Facebook

One thought on “Ribosome tolerates artificial foldamers

  • 7th November 2018 at 5:30 am

    What's up i am kavin, its my first time to commenting anyplace, when i
    read this post i thought i could also create comment due to this
    good post.


Leave a Reply

Your email address will not be published. Required fields are marked *

Enable notifications of new posts OK No thanks