Ribosomal synthesis and folding of peptide-helical aromatic foldamer hybrids

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Ribosomal synthesis and folding of peptide-helical aromatic foldamer hybrids. / Rogers, Joseph M.; Kwon, Sunbum; Dawson, Simon J.; Mandal, Pradeep K.; Suga, Hiroaki; Huc, Ivan.

In: Nature Chemistry, Vol. 10, No. 4, 01.04.2018, p. 405-412.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Rogers, JM, Kwon, S, Dawson, SJ, Mandal, PK, Suga, H & Huc, I 2018, 'Ribosomal synthesis and folding of peptide-helical aromatic foldamer hybrids', Nature Chemistry, vol. 10, no. 4, pp. 405-412. https://doi.org/10.1038/s41557-018-0007-x

APA

Rogers, J. M., Kwon, S., Dawson, S. J., Mandal, P. K., Suga, H., & Huc, I. (2018). Ribosomal synthesis and folding of peptide-helical aromatic foldamer hybrids. Nature Chemistry, 10(4), 405-412. https://doi.org/10.1038/s41557-018-0007-x

Vancouver

Rogers JM, Kwon S, Dawson SJ, Mandal PK, Suga H, Huc I. Ribosomal synthesis and folding of peptide-helical aromatic foldamer hybrids. Nature Chemistry. 2018 Apr 1;10(4):405-412. https://doi.org/10.1038/s41557-018-0007-x

Author

Rogers, Joseph M. ; Kwon, Sunbum ; Dawson, Simon J. ; Mandal, Pradeep K. ; Suga, Hiroaki ; Huc, Ivan. / Ribosomal synthesis and folding of peptide-helical aromatic foldamer hybrids. In: Nature Chemistry. 2018 ; Vol. 10, No. 4. pp. 405-412.

Bibtex

@article{383a09cd409f4bb0844791735fc08319,
title = "Ribosomal synthesis and folding of peptide-helical aromatic foldamer hybrids",
abstract = "Translation, 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. 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.",
author = "Rogers, {Joseph M.} and Sunbum Kwon and Dawson, {Simon J.} and Mandal, {Pradeep K.} and Hiroaki Suga and Ivan Huc",
year = "2018",
month = apr,
day = "1",
doi = "10.1038/s41557-018-0007-x",
language = "English",
volume = "10",
pages = "405--412",
journal = "Nature Chemistry",
issn = "1755-4330",
publisher = "nature publishing group",
number = "4",

}

RIS

TY - JOUR

T1 - Ribosomal synthesis and folding of peptide-helical aromatic foldamer hybrids

AU - Rogers, Joseph M.

AU - Kwon, Sunbum

AU - Dawson, Simon J.

AU - Mandal, Pradeep K.

AU - Suga, Hiroaki

AU - Huc, Ivan

PY - 2018/4/1

Y1 - 2018/4/1

N2 - Translation, 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. 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.

AB - Translation, 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. 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.

UR - http://www.scopus.com/inward/record.url?scp=85044187571&partnerID=8YFLogxK

U2 - 10.1038/s41557-018-0007-x

DO - 10.1038/s41557-018-0007-x

M3 - Journal article

C2 - 29556052

AN - SCOPUS:85044187571

VL - 10

SP - 405

EP - 412

JO - Nature Chemistry

JF - Nature Chemistry

SN - 1755-4330

IS - 4

ER -

ID: 243921896