Novel anti-HIV peptides containing multiple copies of artificially designed heptad repeat motifs
- Beijing Institute of Pharmacology and Toxicology, Pharmaceutical Chemistry, 27 Taiping Road, Beijing 100850 (China)
- Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10065 (United States)
The peptidic anti-HIV drug T20 (Fuzeon) and its analog C34 share a common heptad repeat (HR) sequence, but they have different functional domains, i.e., pocket- and lipid-binding domains (PBD and LBD, respectively). We hypothesize that novel anti-HIV peptides may be designed by using artificial sequences containing multiple copies of HR motifs plus zero, one or two functional domains. Surprisingly, we found that the peptides containing only the non-natural HR sequences could significantly inhibit HIV-1 infection, while addition of PBD and/or LBD to the peptides resulted in significant improvement of anti-HIV-1 activity. These results suggest that these artificial HR sequences, which may serve as structural domains, could be used as templates for the design of novel antiviral peptides against HIV and other viruses with class I fusion proteins.
- OSTI ID:
- 21143889
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 374, Issue 4; Other Information: DOI: 10.1016/j.bbrc.2008.07.134; PII: S0006-291X(08)01462-9; Copyright (c) 2008 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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