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Biosci Rep. 2019 Sep 24;39(9). pii: BSR20192196. doi: 10.1042/BSR20192196. Print 2019 Sep 30.

Trimeric heptad repeat synthetic peptides HR1 and HR2 efficiently inhibit HIV-1 entry.

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INSERM, U1043, CPTP, CHU purpan, Toulouse, France.
CNRS, U5282 CPTP, CHU purpan, Toulouse, France.
Université Paul Sabatier, CPTP, CHU purpan, Toulouse, France.
Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac, 10, Barcelona 08028, Spain.
Laboratory of Cellular and Molecular Immunology, Gavin Herbert Eye Institute, University of California Irvine, School of Medicine, Irvine, CA 92697, United States of America.
Department of Inorganic and Organic Chemistry, University of Barcelona, Martı i Franques 1-11, Barcelona 08028, Spain.
INSERM, U1043, CPTP, CHU purpan, Toulouse, France


The trimeric heptad repeat domains HR1 and HR2 of the human immunodeficiency virus 1 (HIV-1) gp41 play a key role in HIV-1-entry by membrane fusion. To develop efficient inhibitors against this step, the corresponding trimeric-N36 and C34 peptides were designed and synthesized. Analysis by circular dichroism of monomeric and trimeric N36 and C34 peptides showed their capacities to adopt α-helical structures and to establish physical interactions. At the virological level, while trimeric-C34 conserves the same high anti-fusion activity as monomeric-C34, trimerization of N36-peptide induced a significant increase, reaching 500-times higher in anti-fusion activity, against R5-tropic virus-mediated fusion. This result was associated with increased stability of the N36 trimer peptide with respect to the monomeric form, as demonstrated by the comparative kinetics of their antiviral activities during 6-day incubation in a physiological medium. Collectively, our findings demonstrate that while the trimerization of C34 peptide had no beneficial effect on its stability and antiviral activity, the trimerization of N36 peptide strengthened both stability and antiviral activity. This approach, promotes trimers as new promising HIV-1 inhibitors and point to future development aimed toward innovative peptide fusion inhibitors, microbicides or as immunogens.


AIDS; C34; HIV-1; N36; inhibitors; trimers

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