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

RIS ID

99359

Publication Details

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.

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.

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Link to publisher version (DOI)

http://dx.doi.org/10.1016/j.tet.2014.07.096