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Helical cyclic pentapeptides constrain HIV-1 Rev peptide for enhanced RNA binding
- Source :
- Tetrahedron. 70:7645-7650
- Publication Year :
- 2014
- Publisher :
- Elsevier BV, 2014.
-
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.
- Subjects :
- 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
Subjects
Details
- ISSN :
- 00404020
- Volume :
- 70
- Database :
- OpenAIRE
- Journal :
- Tetrahedron
- Accession number :
- edsair.doi...........516e26dde7de4353d59410d906344551