Bioorganic synthesis of a recombinant HIV-1 fusion inhibitor, SC35EK, with an N-terminal pyroglutamate capping group

Kazumi Kajiwara; Kentaro Watanabe; Rei Tokiwa; Tomoko Kurose; Hiroaki Ohno; Hiroko Tsutsumi; Yoji Hata; Kazuki Izumi; Eiichi Kodama; Masao Matsuoka; Shinya Oishi; Nobutaka Fujii

doi:10.1016/j.bmc.2009.10.017

Bioorganic synthesis of a recombinant HIV-1 fusion inhibitor, SC35EK, with an N-terminal pyroglutamate capping group

Kazumi Kajiwara, Kentaro Watanabe, Rei Tokiwa, Tomoko Kurose, Hiroaki Ohno, Hiroko Tsutsumi, Yoji Hata, Kazuki Izumi, Eiichi Kodama, Masao Matsuoka, Shinya Oishi, Nobutaka Fujii

IRIDeS - Disaster Medical Science Division

Research output: Contribution to journal › Article › peer-review

11 Citations (Scopus)

Abstract

The bioorganic synthesis of an end-capped anti-HIV peptide from a recombinant protein was investigated. Cyanogen bromide-mediated cleavage of two Met-Gln sites across the target anti-HIV sequence generated an HIV-1 fusion inhibitor (SC35EK) analog bearing an N-terminal pyroglutamate (pGlu) residue and a C-terminal homoserine lactone (Hsl) residue. The end-capped peptide, pGlu-SC35EK-Hsl, had similar bioactivity and biophysical properties to the parent peptide, and an improved resistance to peptidase-mediated degradation was observed compared with the non-end-capped peptide obtained using standard recombinant technology.

Original language	English
Pages (from-to)	7964-7970
Number of pages	7
Journal	Bioorganic and Medicinal Chemistry
Volume	17
Issue number	23
DOIs	https://doi.org/10.1016/j.bmc.2009.10.017
Publication status	Published - 2009 Dec 1

Keywords

Anti-HIV peptide
Fusion inhibitor
HIV
Pyroglutamate

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.bmc.2009.10.017

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title = "Bioorganic synthesis of a recombinant HIV-1 fusion inhibitor, SC35EK, with an N-terminal pyroglutamate capping group",

abstract = "The bioorganic synthesis of an end-capped anti-HIV peptide from a recombinant protein was investigated. Cyanogen bromide-mediated cleavage of two Met-Gln sites across the target anti-HIV sequence generated an HIV-1 fusion inhibitor (SC35EK) analog bearing an N-terminal pyroglutamate (pGlu) residue and a C-terminal homoserine lactone (Hsl) residue. The end-capped peptide, pGlu-SC35EK-Hsl, had similar bioactivity and biophysical properties to the parent peptide, and an improved resistance to peptidase-mediated degradation was observed compared with the non-end-capped peptide obtained using standard recombinant technology.",

keywords = "Anti-HIV peptide, Fusion inhibitor, HIV, Pyroglutamate",

author = "Kazumi Kajiwara and Kentaro Watanabe and Rei Tokiwa and Tomoko Kurose and Hiroaki Ohno and Hiroko Tsutsumi and Yoji Hata and Kazuki Izumi and Eiichi Kodama and Masao Matsuoka and Shinya Oishi and Nobutaka Fujii",

note = "Funding Information: This work was supported by Science and Technology Incubation Program in Advanced Regions from Japan Science and Technology Agency, and Health and Labour Sciences Research Grants (Research on HIV/AIDS). ",

year = "2009",

month = dec,

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doi = "10.1016/j.bmc.2009.10.017",

language = "English",

volume = "17",

pages = "7964--7970",

journal = "Bioorganic and Medicinal Chemistry",

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T1 - Bioorganic synthesis of a recombinant HIV-1 fusion inhibitor, SC35EK, with an N-terminal pyroglutamate capping group

AU - Kajiwara, Kazumi

AU - Watanabe, Kentaro

AU - Tokiwa, Rei

AU - Kurose, Tomoko

AU - Ohno, Hiroaki

AU - Tsutsumi, Hiroko

AU - Hata, Yoji

AU - Izumi, Kazuki

AU - Kodama, Eiichi

AU - Matsuoka, Masao

AU - Oishi, Shinya

AU - Fujii, Nobutaka

N1 - Funding Information: This work was supported by Science and Technology Incubation Program in Advanced Regions from Japan Science and Technology Agency, and Health and Labour Sciences Research Grants (Research on HIV/AIDS).

PY - 2009/12/1

Y1 - 2009/12/1

N2 - The bioorganic synthesis of an end-capped anti-HIV peptide from a recombinant protein was investigated. Cyanogen bromide-mediated cleavage of two Met-Gln sites across the target anti-HIV sequence generated an HIV-1 fusion inhibitor (SC35EK) analog bearing an N-terminal pyroglutamate (pGlu) residue and a C-terminal homoserine lactone (Hsl) residue. The end-capped peptide, pGlu-SC35EK-Hsl, had similar bioactivity and biophysical properties to the parent peptide, and an improved resistance to peptidase-mediated degradation was observed compared with the non-end-capped peptide obtained using standard recombinant technology.

AB - The bioorganic synthesis of an end-capped anti-HIV peptide from a recombinant protein was investigated. Cyanogen bromide-mediated cleavage of two Met-Gln sites across the target anti-HIV sequence generated an HIV-1 fusion inhibitor (SC35EK) analog bearing an N-terminal pyroglutamate (pGlu) residue and a C-terminal homoserine lactone (Hsl) residue. The end-capped peptide, pGlu-SC35EK-Hsl, had similar bioactivity and biophysical properties to the parent peptide, and an improved resistance to peptidase-mediated degradation was observed compared with the non-end-capped peptide obtained using standard recombinant technology.

KW - Anti-HIV peptide

KW - Fusion inhibitor

KW - HIV

KW - Pyroglutamate

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DO - 10.1016/j.bmc.2009.10.017

M3 - Article

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AN - SCOPUS:72149087467

SN - 0968-0896

VL - 17

SP - 7964

EP - 7970

JO - Bioorganic and Medicinal Chemistry

JF - Bioorganic and Medicinal Chemistry

IS - 23

ER -

Bioorganic synthesis of a recombinant HIV-1 fusion inhibitor, SC35EK, with an N-terminal pyroglutamate capping group

Abstract

Keywords

UN SDGs

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