A single replacement of histidine to arginine in EGFR-lytic hybrid peptide demonstrates the improved anticancer activity

Tada, Noriko; Horibe, Tomohisa; Haramoto, Mari; Ohara, Koji; Kohno, Masayuki; Kawakami, Koji

doi:10.1016/j.bbrc.2011.03.030

Cited by 34 publications

(26 citation statements)

References 26 publications

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“…Arginine (R) is most positively charged of all amino acids (Nakase, Takeuchi, Tanaka, & Futaki, 2008). In a study Tada et al (2011) reported a single replacement of histidine to arginine in EGFRlytic peptide (YHWYGYTPQNVI) improved 1.2-to 1.9-fold higher cytotoxic activity than the original peptide. Nakase et al (2008) revealed that the hydrogen-bond formation of the guanidino moiety in arginine (R) with phosphates, sulfates, and carboxylates on cellular components was proposed to be appreciated for cell-permeation efficacy.…”

Section: Contribution Of Amino Acid Residue To Antiproliferative Actimentioning

confidence: 97%

“…Many cationic peptides would disrupt tumor cells by interacting strongly with the anionic components on cellar membrane (Mader & Hoskin, 2006). The electrostatic attraction was believed to be crucial for cell-permeation efficacy of anticancer peptide (Nakase et al, 2008;Tada et al, 2011). Thus, the enhanced cytotoxicity of YALRAH would be due to its increased cationic charges and hydrogen bonding properties by replacement of proline (P) with arginine (R).…”

Section: Contribution Of Amino Acid Residue To Antiproliferative Actimentioning

confidence: 98%

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Isolation and identification of an antiproliferative peptide derived from heated products of peptic hydrolysates of half-fin anchovy (Setipinna taty)

Song

Wei

Luo

et al. 2014

Journal of Functional Foods

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Section: Contribution Of Amino Acid Residue To Antiproliferative Actimentioning

confidence: 97%

Section: Contribution Of Amino Acid Residue To Antiproliferative Actimentioning

confidence: 98%

Isolation and identification of an antiproliferative peptide derived from heated products of peptic hydrolysates of half-fin anchovy (Setipinna taty)

Song

Wei

Luo

et al. 2014

Journal of Functional Foods

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“…To evaluate the potential use of CMD-s-s-peptide conjugates as effective peptide drug carriers for the therapeutic treatment of tumors in vivo, anti-tumor activity was monitored in a xenografted mice model as previously described [1,2]. The suspension of BxPC-3 cells was subcutaneously transplanted into nude mice (day 0).…”

Section: Evaluation Of In Vivo Anti-tumor Activity Of Cmd-s-s-peptidementioning

confidence: 99%

“…The cells (3000 cells/well seeded in a 96-well plate) were treated with various concentrations of CMD-s-s-peptide conjugates or free peptide for 48 h at 37°C and cell viability was measured using the WST-8 assay, as previously described [1,2].…”

Section: In Vitro Cytotoxicitymentioning

confidence: 99%

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Enhancement of anti-tumor activity of hybrid peptide in conjugation with carboxymethyl dextran via disulfide linkers

Gaowa

Horibe

Kohno

et al. 2015

European Journal of Pharmaceutics and Biopharmaceutics

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Localization of the anti‐cancer peptide EGFR‐lytic hybrid peptide in human pancreatic cancer BxPC‐3 cells by immunocytochemistry

Ohara

Kohno

Kawakami

2013

Journal of Peptide Science

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Cationic lytic-type peptides have been studied for clinical application in various infections and cancers, but their functional cellular mechanisms remain unclear. We generated anti-cancer epithelial growth factor receptor (EGFR)-lytic hybrid peptide, a 32-amino-acid peptide composed of an EGFR-binding sequence and lytic sequence. In this study, we investigated the distribution of EGFR-lytic hybrid peptide in BxPC-3 human pancreatic cancer cells by an immunocytochemical (ICC) method. Distribution of EGFR protein expression was unchanged after treatment with EGFR-lytic peptide compared with non-treated cells. In confocal laser scanning microscopy, immunostaining of EGFR-lytic peptide was observed in the cytoplasm, mostly in the form of granules. Some staining was also localized on the mitochondrial membrane. At the ultrastructure level, cells treated with EGFR-lytic peptide had a low electron density, disappearance of microvilli, and swollen mitochondria. Fragments of cell membrane were also observed in the proximity of the membrane. In immunoelectron microscopy, EGFR-lytic peptide was observed in the cell membrane and cytoplasm. A number of granules were considered swollen mitochondria. Activation of the caspase pathway as a result of mitochondrial dysfunction was also examined to determine the cytotoxic activity of EGFR-lytic peptide; however, no effect on cell death after EGFR-lytic treatment was observed, and moreover, apoptosis was not found to play a critical role in the cell death mechanism. These results suggest that EGFR-lytic peptide is localized on cell and mitochondrial membranes, with disintegration of the cell membrane contributing mainly to cell death.

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A single replacement of histidine to arginine in EGFR-lytic hybrid peptide demonstrates the improved anticancer activity

Cited by 34 publications

References 26 publications

Isolation and identification of an antiproliferative peptide derived from heated products of peptic hydrolysates of half-fin anchovy (Setipinna taty)

Isolation and identification of an antiproliferative peptide derived from heated products of peptic hydrolysates of half-fin anchovy (Setipinna taty)

Enhancement of anti-tumor activity of hybrid peptide in conjugation with carboxymethyl dextran via disulfide linkers

Localization of the anti‐cancer peptide EGFR‐lytic hybrid peptide in human pancreatic cancer BxPC‐3 cells by immunocytochemistry

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