Structure-activity relationship of a novel pentapeptide with cancer cell growth-inhibitory activity

Masakatsu Kamiya; Keisuke Oyauchi; Yoshinori Sato; Takuya Yokoyama; Mofei Wang; Tomoyasu Aizawa; Yasuhiro Kumaki; Mineyuki Mizuguchi; Kunio Imai; Makoto Demura; Koichi Suzuki; Keiichi Kawano

doi:10.1002/psc.1225

Structure-activity relationship of a novel pentapeptide with cancer cell growth-inhibitory activity

Masakatsu Kamiya, Keisuke Oyauchi, Yoshinori Sato, Takuya Yokoyama, Mofei Wang, Tomoyasu Aizawa, Yasuhiro Kumaki, Mineyuki Mizuguchi, Kunio Imai, Makoto Demura, Koichi Suzuki, Keiichi Kawano^*

^*Corresponding author for this work

Structural Biology

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

5 Scopus citations

Abstract

We previously reported that yamamarin, a pentapeptide with an amidated C-terminus (DILRG-NH₂) isolated from larvae of the silkmoth, and its palmitoylated analog (C16-DILRG-NH₂) suppressed proliferation of rat hepatoma (liver cancer) cells. In this study, we investigated the structure-activity relationship of yamamarin by in vitro assay and spectroscopic methods (CD and NMR) for various analogs. The in vitro assay results demonstrated that the chemical structure of the C-terminal part (-RG-NH ₂) of yamamarin is essential for its activity. The CD and NMR results indicated that yamamarin and its analog adopt predominantly a random coil conformation. Moreover, a comparison of NMR spectra of DILRG-NH₂ and C16-DILRG-NH₂ revealed that the N-terminal palmitoyl group of C16-DILRG-NH₂ did not affect the conformation of the C-terminal part, which is essential for activity. Together, these results should assist in the design of more sophisticated anticancer drugs.

Original language	English
Pages (from-to)	242-248
Number of pages	7
Journal	Journal of Peptide Science
Volume	16
Issue number	5
DOIs	https://doi.org/10.1002/psc.1225
State	Published - 2010/05

Keywords

CD
Cell growth suppression
Insect pentapeptide
NMR

ASJC Scopus subject areas

Structural Biology
Biochemistry
Molecular Medicine
Molecular Biology
Pharmacology
Drug Discovery
Organic Chemistry

UN SDGs

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

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10.1002/psc.1225

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title = "Structure-activity relationship of a novel pentapeptide with cancer cell growth-inhibitory activity",

abstract = "We previously reported that yamamarin, a pentapeptide with an amidated C-terminus (DILRG-NH2) isolated from larvae of the silkmoth, and its palmitoylated analog (C16-DILRG-NH2) suppressed proliferation of rat hepatoma (liver cancer) cells. In this study, we investigated the structure-activity relationship of yamamarin by in vitro assay and spectroscopic methods (CD and NMR) for various analogs. The in vitro assay results demonstrated that the chemical structure of the C-terminal part (-RG-NH 2) of yamamarin is essential for its activity. The CD and NMR results indicated that yamamarin and its analog adopt predominantly a random coil conformation. Moreover, a comparison of NMR spectra of DILRG-NH2 and C16-DILRG-NH2 revealed that the N-terminal palmitoyl group of C16-DILRG-NH2 did not affect the conformation of the C-terminal part, which is essential for activity. Together, these results should assist in the design of more sophisticated anticancer drugs.",

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author = "Masakatsu Kamiya and Keisuke Oyauchi and Yoshinori Sato and Takuya Yokoyama and Mofei Wang and Tomoyasu Aizawa and Yasuhiro Kumaki and Mineyuki Mizuguchi and Kunio Imai and Makoto Demura and Koichi Suzuki and Keiichi Kawano",

year = "2010",

month = may,

doi = "10.1002/psc.1225",

language = "英語",

volume = "16",

pages = "242--248",

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T1 - Structure-activity relationship of a novel pentapeptide with cancer cell growth-inhibitory activity

AU - Kamiya, Masakatsu

AU - Oyauchi, Keisuke

AU - Sato, Yoshinori

AU - Yokoyama, Takuya

AU - Wang, Mofei

AU - Aizawa, Tomoyasu

AU - Kumaki, Yasuhiro

AU - Mizuguchi, Mineyuki

AU - Imai, Kunio

AU - Demura, Makoto

AU - Suzuki, Koichi

AU - Kawano, Keiichi

PY - 2010/5

Y1 - 2010/5

N2 - We previously reported that yamamarin, a pentapeptide with an amidated C-terminus (DILRG-NH2) isolated from larvae of the silkmoth, and its palmitoylated analog (C16-DILRG-NH2) suppressed proliferation of rat hepatoma (liver cancer) cells. In this study, we investigated the structure-activity relationship of yamamarin by in vitro assay and spectroscopic methods (CD and NMR) for various analogs. The in vitro assay results demonstrated that the chemical structure of the C-terminal part (-RG-NH 2) of yamamarin is essential for its activity. The CD and NMR results indicated that yamamarin and its analog adopt predominantly a random coil conformation. Moreover, a comparison of NMR spectra of DILRG-NH2 and C16-DILRG-NH2 revealed that the N-terminal palmitoyl group of C16-DILRG-NH2 did not affect the conformation of the C-terminal part, which is essential for activity. Together, these results should assist in the design of more sophisticated anticancer drugs.

AB - We previously reported that yamamarin, a pentapeptide with an amidated C-terminus (DILRG-NH2) isolated from larvae of the silkmoth, and its palmitoylated analog (C16-DILRG-NH2) suppressed proliferation of rat hepatoma (liver cancer) cells. In this study, we investigated the structure-activity relationship of yamamarin by in vitro assay and spectroscopic methods (CD and NMR) for various analogs. The in vitro assay results demonstrated that the chemical structure of the C-terminal part (-RG-NH 2) of yamamarin is essential for its activity. The CD and NMR results indicated that yamamarin and its analog adopt predominantly a random coil conformation. Moreover, a comparison of NMR spectra of DILRG-NH2 and C16-DILRG-NH2 revealed that the N-terminal palmitoyl group of C16-DILRG-NH2 did not affect the conformation of the C-terminal part, which is essential for activity. Together, these results should assist in the design of more sophisticated anticancer drugs.

KW - CD

KW - Cell growth suppression

KW - Insect pentapeptide

KW - NMR

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DO - 10.1002/psc.1225

M3 - 学術論文

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AN - SCOPUS:77951124462

SN - 1075-2617

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JF - Journal of Peptide Science

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ER -

Structure-activity relationship of a novel pentapeptide with cancer cell growth-inhibitory activity

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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