Skip to main content
placeholder image

Helical cyclic pentapeptides constrain HIV-1 Rev peptide for enhanced RNA binding

Journal Article


Abstract


  • HIV-1 Rev is a 116 residue transporter protein that enters the host cell nucleus and uses its 17 amino acid segment (Rev34–50) to bind and capture a specific piece of RNA, the Rev Response Element (RRE), for transport to the cytoplasm. This is critical for HIV replication. In isolation, Rev34–50 shows negligible structure in water, but is alpha helical in a mixture of water and 2,2,2-trifluoroethanol (TFE) or when bound to RRE. Here we report that helix-constrained cyclic pentapeptides, either appended to the N-terminus or incorporated within Rev34–50, are efficient helix nucleators in water. They induce up to 90% alpha helicity for isolated Rev peptides in water and confer high RNA-binding affinity.

Authors


  •   Harrison, Rosemary S. (external author)
  •   Shepherd, Nicholas E. (external author)
  •   Hoang, Huy N. (external author)
  •   Beyer, Renee L. (external author)
  •   Ruiz-Gomez, Gloria (external author)
  •   Kelso, Michael J.
  •   Mei Kok, W (external author)
  •   Hill, Timothy A. (external author)
  •   Abbenante, Giovanni (external author)
  •   Fairlie, David P. (external author)

Publication Date


  • 2014

Citation


  • Harrison, R. S., Shepherd, N. E., Hoang, H. N., Beyer, R. L., Ruiz-Gomez, G., Kelso, M. J., Mei Kok, W., Hill, T. A., Abbenante, G. & Fairlie, D. P. (2014). Helical cyclic pentapeptides constrain HIV-1 Rev peptide for enhanced RNA binding. Tetrahedron: the international journal for the rapid publication of full original research papers and critical reviews in organic chemistry, 70 (42), 7645-7650.

Scopus Eid


  • 2-s2.0-84907935289

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/2665

Number Of Pages


  • 5

Start Page


  • 7645

End Page


  • 7650

Volume


  • 70

Issue


  • 42

Abstract


  • HIV-1 Rev is a 116 residue transporter protein that enters the host cell nucleus and uses its 17 amino acid segment (Rev34–50) to bind and capture a specific piece of RNA, the Rev Response Element (RRE), for transport to the cytoplasm. This is critical for HIV replication. In isolation, Rev34–50 shows negligible structure in water, but is alpha helical in a mixture of water and 2,2,2-trifluoroethanol (TFE) or when bound to RRE. Here we report that helix-constrained cyclic pentapeptides, either appended to the N-terminus or incorporated within Rev34–50, are efficient helix nucleators in water. They induce up to 90% alpha helicity for isolated Rev peptides in water and confer high RNA-binding affinity.

Authors


  •   Harrison, Rosemary S. (external author)
  •   Shepherd, Nicholas E. (external author)
  •   Hoang, Huy N. (external author)
  •   Beyer, Renee L. (external author)
  •   Ruiz-Gomez, Gloria (external author)
  •   Kelso, Michael J.
  •   Mei Kok, W (external author)
  •   Hill, Timothy A. (external author)
  •   Abbenante, Giovanni (external author)
  •   Fairlie, David P. (external author)

Publication Date


  • 2014

Citation


  • Harrison, R. S., Shepherd, N. E., Hoang, H. N., Beyer, R. L., Ruiz-Gomez, G., Kelso, M. J., Mei Kok, W., Hill, T. A., Abbenante, G. & Fairlie, D. P. (2014). Helical cyclic pentapeptides constrain HIV-1 Rev peptide for enhanced RNA binding. Tetrahedron: the international journal for the rapid publication of full original research papers and critical reviews in organic chemistry, 70 (42), 7645-7650.

Scopus Eid


  • 2-s2.0-84907935289

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/2665

Number Of Pages


  • 5

Start Page


  • 7645

End Page


  • 7650

Volume


  • 70

Issue


  • 42