Helical cyclic pentapeptides constrain HIV-1 Rev peptide for enhanced RNA binding
| Autor: | David P. Fairlie, Michael J. Kelso, Timothy A. Hill, Huy N. Hoang, Nicholas E. Shepherd, W. Mei Kok, Gloria Ruiz-Gómez, Rosemary S. Harrison, Giovanni Abbenante, Renee L. Beyer |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences viruses Organic Chemistry RNA Peptide 010402 general chemistry 01 natural sciences Biochemistry Cyclic peptide 3. Good health 0104 chemical sciences Amino acid 03 medical and health sciences chemistry Cytoplasm Drug Discovery Helix Biophysics Host cell nucleus Alpha helix 030304 developmental biology |
| Zdroj: | Tetrahedron. 70:7645-7650 |
| ISSN: | 0040-4020 |
| DOI: | 10.1016/j.tet.2014.07.096 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect