Design and evaluation of antiretroviral peptides corresponding to the C-terminal heptad repeat region (C-HR) of human immunodeficiency virus type 1 envelope glycoprotein gp41
| Autor: | Kazuyoshi Ikuta, Yu-Shi Tian, Piraporn Utachee, Bongkot Soonthornsata, Sompong Sapsutthipas, Norihito Kawashita, Panasda Isarangkura-na-ayuthaya, Pathom Sawanpanyalert, Masanori Kameoka, Tatsuya Takagi, Wattana Auwanit |
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| Rok vydání: | 2010 |
| Předmět: |
Models
Molecular Protein Conformation viruses Molecular Sequence Data α-helical heptad repeat Peptide Biology Virus Replication Gp41 Virus C34 fusion inhibitor Virology CRF01_AE Amino Acid Sequence Peptide sequence Subtypes chemistry.chemical_classification Lipid bilayer fusion HIV Envelope Protein gp41 Peptide Fragments Heptad repeat Anti-Retroviral Agents chemistry Viral replication Drug Design HIV-1 Envelope glycoprotein gp41 Peptides Glycoprotein |
| Zdroj: | Virology. 405:157-164 |
| ISSN: | 0042-6822 |
| Popis: | Two α-helical heptad repeats, N-HR and C-HR, located in the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein gp41, play an important role in membrane fusion by forming a 6-helix bundle. C34, a peptide mimicking C-HR, inhibits the formation of the 6-helix bundle; thus, it has potential as a novel antiretroviral compound. In order to improve the inhibitory effect of C34 on HIV-1 replication, we designed new C34-derived peptides based on computational analysis of the stable conformation of the 6-helix bundle. Newly designed peptides showed a stronger inhibitory effect on the replication of recombinant viruses containing CRF01_AE, subtype B or subtype C Env than C34 or a fusion inhibitor, T-20. In addition, these peptides inhibited the replication of a T-20-resistant virus. We propose that these peptides could be applied to develop novel antiretroviral compounds to inhibit the replication of various subtypes of HIV-1 as well as of T-20-resistant variants. |
| Databáze: | OpenAIRE |
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