SC29EK, a Peptide Fusion Inhibitor with Enhanced α-Helicity, Inhibits Replication of Human Immunodeficiency Virus Type 1 Mutants Resistant to Enfuvirtide
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| Published in | Antimicrobial Agents and Chemotherapy Vol. 53; no. 3; pp. 1013 - 1018 |
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| Main Authors | , , , , , , , , , , |
| Format | Journal Article |
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American Society for Microbiology
01.03.2009
American Society for Microbiology (ASM) |
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| AbstractList | Peptides derived from the alpha-helical domains of human immunodeficiency virus (HIV) type 1 (HIV-1) gp41 inhibit HIV-1 fusion to the cell membrane. Enfuvirtide (T-20) is a peptide-based drug that targets the step of HIV fusion, and as such, it effectively suppresses the replication of HIV-1 strains that are either wild type or resistant to multiple reverse transcriptase and/or protease inhibitors. However, HIV-1 variants with T-20 resistance have emerged; therefore, the development of new and potent inhibitors is urgently needed. We have developed a novel HIV fusion inhibitor, SC34EK, which is a gp41-derived 34-amino-acid peptide with glutamate (E) and lysine (K) substitutions on its solvent-accessible site that stabilize its alpha-helicity. Importantly, SC34EK effectively inhibits the replication of T-20-resistant HIV-1 strains as well as wild-type HIV-1. In this report, we introduce SC29EK, a 29-amino-acid peptide that is a shorter variant of SC34EK. SC29EK blocked the replication of T-20-resistant HIV-1 strains and maintained antiviral activity even in the presence of high serum concentrations (up to 50%). Circular dichroism analysis revealed that the alpha-helicity of SC29EK was well maintained, while that of the parental peptide, C29, which showed moderate and reduced inhibition of wild-type and T-20-resistant HIV-1 strains, was lower. Our results show that the alpha-helicity in a peptide-based fusion inhibitor is a key factor for activity and enables the design of short peptide inhibitors with improved pharmacological properties. Peptides derived from the α-helical domains of human immunodeficiency virus (HIV) type 1 (HIV-1) gp41 inhibit HIV-1 fusion to the cell membrane. Enfuvirtide (T-20) is a peptide-based drug that targets the step of HIV fusion, and as such, it effectively suppresses the replication of HIV-1 strains that are either wild type or resistant to multiple reverse transcriptase and/or protease inhibitors. However, HIV-1 variants with T-20 resistance have emerged; therefore, the development of new and potent inhibitors is urgently needed. We have developed a novel HIV fusion inhibitor, SC34EK, which is a gp41-derived 34-amino-acid peptide with glutamate (E) and lysine (K) substitutions on its solvent-accessible site that stabilize its α-helicity. Importantly, SC34EK effectively inhibits the replication of T-20-resistant HIV-1 strains as well as wild-type HIV-1. In this report, we introduce SC29EK, a 29-amino-acid peptide that is a shorter variant of SC34EK. SC29EK blocked the replication of T-20-resistant HIV-1 strains and maintained antiviral activity even in the presence of high serum concentrations (up to 50%). Circular dichroism analysis revealed that the α-helicity of SC29EK was well maintained, while that of the parental peptide, C29, which showed moderate and reduced inhibition of wild-type and T-20-resistant HIV-1 strains, was lower. Our results show that the α-helicity in a peptide-based fusion inhibitor is a key factor for activity and enables the design of short peptide inhibitors with improved pharmacological properties. Classifications Services AAC Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue AAC About AAC Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy AAC RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0066-4804 Online ISSN: 1098-6596 Copyright © 2014 by the American Society for Microbiology. For an alternate route to AAC .asm.org, visit: AAC ABSTRACT Peptides derived from the α-helical domains of human immunodeficiency virus (HIV) type 1 (HIV-1) gp41 inhibit HIV-1 fusion to the cell membrane. Enfuvirtide (T-20) is a peptide-based drug that targets the step of HIV fusion, and as such, it effectively suppresses the replication of HIV-1 strains that are either wild type or resistant to multiple reverse transcriptase and/or protease inhibitors. However, HIV-1 variants with T-20 resistance have emerged; therefore, the development of new and potent inhibitors is urgently needed. We have developed a novel HIV fusion inhibitor, SC34EK, which is a gp41-derived 34-amino-acid peptide with glutamate (E) and lysine (K) substitutions on its solvent-accessible site that stabilize its α-helicity. Importantly, SC34EK effectively inhibits the replication of T-20-resistant HIV-1 strains as well as wild-type HIV-1. In this report, we introduce SC29EK, a 29-amino-acid peptide that is a shorter variant of SC34EK. SC29EK blocked the replication of T-20-resistant HIV-1 strains and maintained antiviral activity even in the presence of high serum concentrations (up to 50%). Circular dichroism analysis revealed that the α-helicity of SC29EK was well maintained, while that of the parental peptide, C29, which showed moderate and reduced inhibition of wild-type and T-20-resistant HIV-1 strains, was lower. Our results show that the α-helicity in a peptide-based fusion inhibitor is a key factor for activity and enables the design of short peptide inhibitors with improved pharmacological properties. |
| Author | Keiko Kajiwara Kazuki Izumi Hiroki Nishikawa Nobutaka Fujii Shinya Oishi Stefan G. Sarafianos Takeshi Naito Yasuko Sakagami Kentaro Watanabe Masao Matsuoka Eiichi Kodama |
| AuthorAffiliation | Laboratory of Virus Control, Institute for Virus Research, Kyoto University, 53 Kawaramachi, Shogoin, Sakyo-ku, Kyoto 606-8507, Japan, 1 Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan, 2 Department of Molecular Microbiology and Immunology, University of Missouri School of Medicine, Columbia, Missouri 3 |
| AuthorAffiliation_xml | – name: Laboratory of Virus Control, Institute for Virus Research, Kyoto University, 53 Kawaramachi, Shogoin, Sakyo-ku, Kyoto 606-8507, Japan, 1 Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan, 2 Department of Molecular Microbiology and Immunology, University of Missouri School of Medicine, Columbia, Missouri 3 |
| Author_xml | – sequence: 1 givenname: Takeshi surname: NAITO fullname: NAITO, Takeshi organization: Laboratory of Virus Control, Institute for Virus Research, Kyoto University, 53 Kawaramachi, Shogoin, Sakyo-ku, Kyoto 606-8507, Japan – sequence: 2 givenname: Kazuki surname: IZUMI fullname: IZUMI, Kazuki organization: Laboratory of Virus Control, Institute for Virus Research, Kyoto University, 53 Kawaramachi, Shogoin, Sakyo-ku, Kyoto 606-8507, Japan – sequence: 3 givenname: Masao surname: MATSUOKA fullname: MATSUOKA, Masao organization: Laboratory of Virus Control, Institute for Virus Research, Kyoto University, 53 Kawaramachi, Shogoin, Sakyo-ku, Kyoto 606-8507, Japan – sequence: 4 givenname: Eiichi surname: KODAMA fullname: KODAMA, Eiichi organization: Laboratory of Virus Control, Institute for Virus Research, Kyoto University, 53 Kawaramachi, Shogoin, Sakyo-ku, Kyoto 606-8507, Japan – sequence: 5 givenname: Yasuko surname: SAKAGAMI fullname: SAKAGAMI, Yasuko organization: Laboratory of Virus Control, Institute for Virus Research, Kyoto University, 53 Kawaramachi, Shogoin, Sakyo-ku, Kyoto 606-8507, Japan – sequence: 6 givenname: Keiko surname: KAJIWARA fullname: KAJIWARA, Keiko organization: Laboratory of Virus Control, Institute for Virus Research, Kyoto University, 53 Kawaramachi, Shogoin, Sakyo-ku, Kyoto 606-8507, Japan – sequence: 7 givenname: Hiroki surname: NISHIKAWA fullname: NISHIKAWA, Hiroki organization: Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan – sequence: 8 givenname: Kentaro surname: WATANABE fullname: WATANABE, Kentaro organization: Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan – sequence: 9 givenname: Stefan G surname: SARAFIANOS fullname: SARAFIANOS, Stefan G organization: Department of Molecular Microbiology and Immunology, University of Missouri School of Medicine, Columbia, Missouri, United States – sequence: 10 givenname: Shinya surname: OISHI fullname: OISHI, Shinya organization: Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan – sequence: 11 givenname: Nobutaka surname: FUJII fullname: FUJII, Nobutaka organization: Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan |
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| Cites_doi | 10.1128/jvi.66.4.2232-2239.1992 10.1056/NEJMoa035211 10.1128/JVI.78.9.4628-4637.2004 10.1021/jm701109d 10.1128/AAC.46.6.1896-1905.2002 10.1089/aid.1993.9.1051 10.1093/jb/mvh048 10.1128/JVI.72.2.986-993.1998 10.1056/NEJMoa035026 10.1073/pnas.84.24.8898 10.1128/JVI.02706-05 10.1073/pnas.0601036103 10.1128/JVI.79.2.764-770.2005 10.1080/07391102.1997.10508958 10.1002/1521-3773(20020816)41:16<2937::AID-ANIE2937>3.0.CO;2-J 10.1128/JVI.73.10.8578-8586.1999 10.1016/0378-1119(94)90641-6 10.1086/381707 10.1097/00002030-200209270-00014 10.1073/pnas.95.26.15613 10.1073/pnas.0406696101 10.1128/JVI.79.10.5996-6004.2005 10.1016/S0092-8674(00)81430-0 10.1073/pnas.232566599 10.1016/S0092-8674(00)80205-6 10.1128/AAC.46.12.3954-3962.2002 10.1073/pnas.0701478104 10.1128/JVI.79.19.12447-12454.2005 10.1128/jvi.59.2.284-291.1986 10.1128/AAC.48.11.4349-4359.2004 10.1128/AAC.49.3.1113-1119.2005 |
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| Keywords | Immunopathology Antiretroviral agent Peptides HIV-1 virus Retroviridae AIDS Immune deficiency Lentivirus Fusion inhibitor Infection Virus Resistance Enfuvirtide Viral disease Antiviral Replication Human immunodeficiency virus Mutation |
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| Notes | Corresponding author. Mailing address: Laboratory of Virus Control, Institute for Virus Research, Kyoto University, 53 Kawaramachi, Shogoin, Sakyo-ku, Kyoto 606-8507, Japan. Phone and Fax: 81-75-751-3986. E-mail: ekodama@virus.kyoto-u.ac.jp |
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| References | 9444991 - J Virol. 1998 Feb;72(2):986-93 15857986 - J Virol. 2005 May;79(10):5996-6004 15504864 - Antimicrob Agents Chemother. 2004 Nov;48(11):4349-59 7828859 - Gene. 1994 Dec 30;151(1-2):119-23 15469910 - Proc Natl Acad Sci U S A. 2004 Oct 19;101(42):15046-51 16160172 - J Virol. 2005 Oct;79(19):12447-54 14999611 - J Infect Dis. 2004 Mar 15;189(6):1075-83 12203417 - Angew Chem Int Ed Engl. 2002 Aug 16;41(16):2937-40 12435701 - Antimicrob Agents Chemother. 2002 Dec;46(12):3954-62 15113839 - J Biochem. 2004 Mar;135(3):405-11 9108481 - Cell. 1997 Apr 18;89(2):263-73 1548759 - J Virol. 1992 Apr;66(4):2232-9 15728911 - Antimicrob Agents Chemother. 2005 Mar;49(3):1113-9 12417739 - Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):14664-9 8312047 - AIDS Res Hum Retroviruses. 1993 Nov;9(11):1051-3 16912327 - J Virol. 2006 Sep;80(17):8807-19 18197613 - J Med Chem. 2008 Feb 14;51(3):388-91 3122208 - Proc Natl Acad Sci U S A. 1987 Dec;84(24):8898-902 12351957 - AIDS. 2002 Sep 27;16(14):1959-61 15613304 - J Virol. 2005 Jan;79(2):764-70 12019106 - Antimicrob Agents Chemother. 2002 Jun;46(6):1896-905 9630213 - Cell. 1998 May 29;93(5):681-4 9861018 - Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15613-7 18834950 - Int J Biochem Cell Biol. 2009 Apr;41(4):891-9 17640899 - Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7 12773645 - N Engl J Med. 2003 May 29;348(22):2186-95 3016298 - J Virol. 1986 Aug;59(2):284-91 10482611 - J Virol. 1999 Oct;73(10):8578-86 9439994 - J Biomol Struct Dyn. 1997 Dec;15(3):465-71 15078945 - J Virol. 2004 May;78(9):4628-37 16963566 - Proc Natl Acad Sci U S A. 2006 Sep 19;103(38):13938-43 12637625 - N Engl J Med. 2003 May 29;348(22):2175-85 11399967 - AIDS. 2001 May 4;15(7):935-6 e_1_3_2_26_2 e_1_3_2_27_2 e_1_3_2_28_2 e_1_3_2_29_2 e_1_3_2_22_2 e_1_3_2_23_2 e_1_3_2_24_2 (e_1_3_2_34_2) 2001; 15 e_1_3_2_9_2 e_1_3_2_15_2 e_1_3_2_8_2 e_1_3_2_16_2 e_1_3_2_7_2 e_1_3_2_17_2 e_1_3_2_6_2 e_1_3_2_18_2 e_1_3_2_19_2 e_1_3_2_30_2 e_1_3_2_32_2 e_1_3_2_10_2 (e_1_3_2_25_2) 2008; 51 e_1_3_2_31_2 e_1_3_2_5_2 e_1_3_2_11_2 e_1_3_2_4_2 e_1_3_2_12_2 e_1_3_2_33_2 e_1_3_2_3_2 e_1_3_2_13_2 e_1_3_2_2_2 e_1_3_2_14_2 (e_1_3_2_20_2) 1987; 84 (e_1_3_2_21_2) 2004; 135 |
| References_xml | – ident: e_1_3_2_13_2 doi: 10.1128/jvi.66.4.2232-2239.1992 – ident: e_1_3_2_17_2 doi: 10.1056/NEJMoa035211 – ident: e_1_3_2_18_2 doi: 10.1128/JVI.78.9.4628-4637.2004 – volume: 51 start-page: 388 year: 2008 ident: e_1_3_2_25_2 publication-title: J. Med. Chem. doi: 10.1021/jm701109d – ident: e_1_3_2_30_2 doi: 10.1128/AAC.46.6.1896-1905.2002 – ident: e_1_3_2_32_2 doi: 10.1089/aid.1993.9.1051 – volume: 135 start-page: 405 year: 2004 ident: e_1_3_2_21_2 publication-title: J. Biochem. doi: 10.1093/jb/mvh048 – ident: e_1_3_2_28_2 doi: 10.1128/JVI.72.2.986-993.1998 – ident: e_1_3_2_16_2 doi: 10.1056/NEJMoa035026 – volume: 84 start-page: 8898 year: 1987 ident: e_1_3_2_20_2 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.84.24.8898 – ident: e_1_3_2_15_2 doi: 10.1128/JVI.02706-05 – ident: e_1_3_2_10_2 doi: 10.1073/pnas.0601036103 – ident: e_1_3_2_23_2 doi: 10.1128/JVI.79.2.764-770.2005 – ident: e_1_3_2_19_2 doi: 10.1080/07391102.1997.10508958 – ident: e_1_3_2_26_2 doi: 10.1002/1521-3773(20020816)41:16<2937::AID-ANIE2937>3.0.CO;2-J – ident: e_1_3_2_11_2 doi: 10.1128/JVI.73.10.8578-8586.1999 – ident: e_1_3_2_31_2 doi: 10.1016/0378-1119(94)90641-6 – ident: e_1_3_2_8_2 doi: 10.1086/381707 – ident: e_1_3_2_27_2 doi: 10.1097/00002030-200209270-00014 – ident: e_1_3_2_3_2 doi: 10.1073/pnas.95.26.15613 – ident: e_1_3_2_6_2 doi: 10.1073/pnas.0406696101 – ident: e_1_3_2_14_2 doi: 10.1128/JVI.79.10.5996-6004.2005 – ident: e_1_3_2_5_2 doi: 10.1016/S0092-8674(00)81430-0 – ident: e_1_3_2_29_2 doi: 10.1073/pnas.232566599 – volume: 15 start-page: 935 year: 2001 ident: e_1_3_2_34_2 publication-title: AIDS – ident: e_1_3_2_4_2 doi: 10.1016/S0092-8674(00)80205-6 – ident: e_1_3_2_9_2 doi: 10.1128/AAC.46.12.3954-3962.2002 – ident: e_1_3_2_24_2 – ident: e_1_3_2_7_2 doi: 10.1073/pnas.0701478104 – ident: e_1_3_2_22_2 doi: 10.1128/JVI.79.19.12447-12454.2005 – ident: e_1_3_2_2_2 doi: 10.1128/jvi.59.2.284-291.1986 – ident: e_1_3_2_12_2 doi: 10.1128/AAC.48.11.4349-4359.2004 – ident: e_1_3_2_33_2 doi: 10.1128/AAC.49.3.1113-1119.2005 |
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Reddit... Peptides derived from the alpha-helical domains of human immunodeficiency virus (HIV) type 1 (HIV-1) gp41 inhibit HIV-1 fusion to the cell membrane.... Peptides derived from the α-helical domains of human immunodeficiency virus (HIV) type 1 (HIV-1) gp41 inhibit HIV-1 fusion to the cell membrane. Enfuvirtide... ABSTRACT Peptides derived from the α-helical domains of human immunodeficiency virus (HIV) type 1 (HIV-1) gp41 inhibit HIV-1 fusion to the cell membrane.... |
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| SubjectTerms | Amino Acid Sequence Amino Acid Substitution - drug effects Antibiotics. Antiinfectious agents. Antiparasitic agents Antiviral Agents Biological and medical sciences Circular Dichroism Drug Resistance, Viral Drug Resistance, Viral - drug effects Drug Resistance, Viral - genetics HeLa Cells HIV Envelope Protein gp41 HIV Fusion Inhibitors HIV Fusion Inhibitors - chemistry HIV Fusion Inhibitors - pharmacology HIV-1 HIV-1 - drug effects HIV-1 - genetics HIV-1 - physiology Human viral diseases Humans Immunodeficiencies Immunodeficiencies. Immunoglobulinopathies Immunopathology Infectious diseases Medical sciences Molecular Sequence Data Peptide Fragments Peptides Peptides - chemistry Peptides - pharmacology Pharmacology. Drug treatments Protein Structure, Secondary - genetics Viral diseases Viral diseases of the lymphoid tissue and the blood. Aids Virus Replication Virus Replication - drug effects |
| Title | SC29EK, a Peptide Fusion Inhibitor with Enhanced α-Helicity, Inhibits Replication of Human Immunodeficiency Virus Type 1 Mutants Resistant to Enfuvirtide |
| URI | http://aac.asm.org/content/53/3/1013.abstract https://www.ncbi.nlm.nih.gov/pubmed/19114674 https://journals.asm.org/doi/10.1128/AAC.01211-08 https://pubmed.ncbi.nlm.nih.gov/PMC2650564 |
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