Inhibitory effects of a novel cationic dodecapeptide [CL(14–25)] derived from cyanate lyase of rice on endotoxic activities of LPSs from Escherichia coli and periodontopathic Aggregatibacter actinomycetemcomitans

Takayama, S; Hashimoto, Kenji; Kokubu, Eitoyo; Taniguchi, Masayuki; Tajima, Kouji; Ochiai, Akihito; Saitoh, Eiichi; Saitô, Atsushi; Ishihara, Kazuyuki; Kato, Tsuyoshi

doi:10.1016/j.micpath.2015.08.011

Cited by 9 publications

(31 citation statements)

References 48 publications

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“…Thus, these results illustrated that CL(14-25) exhibits endotoxin-neutralizing activity, similarly as human LL37 [25,27] and ␤-defensins [24,41]. Our previous findings demonstrated that CL(14-25) is a potent, multiple-function, host defense peptide candidate [45,46,48,49].…”

Section: Introductionsupporting

confidence: 55%

“…Mouse macrophages (RAW264) were purchased from RIKEN Bioresource Center (Tsukuba, Ibaraki, Japan) and cultured in DMEM (12,430-54, Invitrogen, CA, USA) supplemented with 10% fetal bovine serum and antibiotic solution (15,140-148, Invitrogen; 100 units/mL penicillin and 100 g/mL streptomycin) in a 5% CO 2 atmosphere at 37 • C [45]. The cells were detached using a cell scraper (3010, Corning Incorporated, NY) and washed once with DMEM.…”

Section: Effect Of Amyi-1-18 On No Production Induced By Endotoxins Amentioning

confidence: 99%

“…The microplates were incubated for 24 h in a 5% CO 2 atmosphere at 37 • C. After removing the culture medium, the cells were stimulated with smooth-type LPS (100 ng/mL), Rc-type LPS (100 ng/mL), or lipid A (100 ng/mL) in the absence or presence of AmyI-1-18 at different concentrations, and the microplates were further incubated for 24 h. The wells containing cells without endotoxin were used as controls. The amount of NO in the medium was estimated from the accumulation of the stable NO metabolite nitrite with Griess reagent (344-07991, Dojindo Laboratories Co., Kumamoto, Japan) according to the manufacturer's instructions [11,45]. Absorbance was measured at 540 nm using a microplate reader (2030 ARVO TM X3; PerkinElmer, MA).…”

Section: Effect Of Amyi-1-18 On No Production Induced By Endotoxins Amentioning

confidence: 99%

“…In our previous studies [46,48,49], we reported that CL(14-25), a novel cationic ␣-helical dodecapeptide of cyanate lyase from rice (Oryza sativa L. japonica), exhibited both arginine-specific cysteine proteinase (Arg-gingipain)-inhibitory activity and antimicrobial activity against Porphyromonas gingivalis, a major etiological agent in the onset and progress of chronic periodontitis. We also investigated the inhibitory ability of CL (14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25) against the endotoxic activities of LPSs from Escherichia coli and periodontopathic Aggregatibacter actinomycetemcomitans [45].…”

Section: Introductionmentioning

confidence: 99%

“…We also investigated the inhibitory ability of CL (14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25) against the endotoxic activities of LPSs from Escherichia coli and periodontopathic Aggregatibacter actinomycetemcomitans [45]. We found that CL (14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25) could inhibit both LPS-induced IL-6 production in human aortic endothelial cells and LPS-induced NO production in mouse macrophages (RAW264).…”

Section: Introductionmentioning

confidence: 99%

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Endotoxin-neutralizing activity and mechanism of action of a cationic α-helical antimicrobial octadecapeptide derived from α-amylase of rice

et al. 2016

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Section: Introductionsupporting

confidence: 55%

Section: Effect Of Amyi-1-18 On No Production Induced By Endotoxins Amentioning

confidence: 99%

Section: Effect Of Amyi-1-18 On No Production Induced By Endotoxins Amentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Endotoxin-neutralizing activity and mechanism of action of a cationic α-helical antimicrobial octadecapeptide derived from α-amylase of rice

et al. 2016

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Identification and characterization of multifunctional cationic and amphipathic peptides from soybean proteins

et al. 2017

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In this study, we identified and chemically synthesized three cationic and amphipathic peptides (Glycinin-17, BCAS-16, and BCBS-11) from soybean proteins. These peptides had high isoelectric points, high positive net charges, and included multiple hydrophobic amino acids. Subsequently, we identified multiple functions of these peptides, including antimicrobial, lipopolysaccharide-neutralizing, and angiogenic activities, and examined their cytotoxic activities against mammalian red blood cells. Glycinin-17, BCAS-16, and BCBS-11 exhibited antimicrobial activity against Porphyromonas gingivalis and Candida albicans whereas Glycinin-17 did not possess antimicrobial effects on Propionibacterium acnes and Streptococcus mutans. Membrane-depolarization assays and flow cytometric analyses showed that the antimicrobial properties of Glycinin-17, BCAS-16, and BCBS-11 against P. gingivalis, P. acnes, and S. mutans were dependent on membrane-disrupting potential. In contrast, major antimicrobial activities of these peptides against C. albicans were dependent on interactions with targets other than cell membranes. Furthermore, chromogenic Limulus amebocyte lysate assays showed that 50% effective concentrations (EC , 0.12-0.31 μM) of these three peptides neutralize LPS with similar potency (EC : 0.11 μM) to that of polymyxin B. Moreover, tube-formation assays in human umbilical vein endothelial cells showed similar angiogenic activities of the three peptides as that following treatment with LL-37. Although BCAS-16 exhibited hemolytic activity, the rate of hemolysis for Glycinin-17 and BCBS-11 in the presence of 500-μM Glycinin-17 and BCBS-11 was less than 2%. These results demonstrate that cationic and amphipathic peptides from soybean proteins, particularly Glycinin-17 and BCBS-11, have potential as multifunctional ingredients for healthcare applications.

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Effects of arginine and leucine substitutions on anti‐endotoxic activities and mechanisms of action of cationic and amphipathic antimicrobial octadecapeptide from rice α‐amylase

Taniguchi

Ochiai

Toyoda

et al. 2017

Journal of Peptide Science

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Previously, we showed that the antimicrobial cationic and amphipathic octadecapeptide AmyI-1-18 from rice α-amylase (AmyI-1) inhibited the endotoxic activity of lipopolysaccharide (LPS) from Escherichia coli. In addition, we demonstrated that several AmyI-1-18 analogs containing arginine or leucine substitutions, which were designed on the basis of the helical wheel projection of AmyI-1-18, exhibited higher antimicrobial activity against human pathogenic microorganisms than AmyI-1-18. In the present study, anti-inflammatory (anti-endotoxic) activities of five AmyI-1-18 analogs containing arginine or leucine substitutions were investigated. Two single arginine-substituted and two single leucine-substituted AmyI-1-18 analogs inhibited the production of LPS-induced nitric oxide in mouse macrophages (RAW264) more effectively than AmyI-1-18. These data indicate that enhanced cationic and hydrophobic properties of AmyI-1-18 are associated with improved anti-endotoxic activity. In subsequent chromogenic Limulus amebocyte lysate assays, 50% inhibitory concentrations (IC ) of the three AmyI-1-18 analogs (G12R, D15R, and E9L) were 0.11-0.13 μm, indicating higher anti-endotoxic activity than that of AmyI-1-18 (IC 0.22 μm), and specific LPS binding activity. In agreement, surface plasmon resonance analyses confirmed direct LPS binding of three AmyI-1-18 analogs. In addition, AmyI-1-18 analogs exhibited little or no cytotoxic activity against RAW264 cells, indicating that enhancements of anti-inflammatory and LPS-neutralizing activities following replacement of arginine or leucine did not result in significant increases in cytotoxicity. This study shows that the arginine-substituted and leucine-substituted AmyI-1-18 analogs with improved anti-endotoxic and antimicrobial activities have clinical potential as dual-function host defense agents. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.

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Inhibitory effects of a novel cationic dodecapeptide [CL(14–25)] derived from cyanate lyase of rice on endotoxic activities of LPSs from Escherichia coli and periodontopathic Aggregatibacter actinomycetemcomitans

Cited by 9 publications

References 48 publications

Endotoxin-neutralizing activity and mechanism of action of a cationic α-helical antimicrobial octadecapeptide derived from α-amylase of rice

Endotoxin-neutralizing activity and mechanism of action of a cationic α-helical antimicrobial octadecapeptide derived from α-amylase of rice

Identification and characterization of multifunctional cationic and amphipathic peptides from soybean proteins

Effects of arginine and leucine substitutions on anti‐endotoxic activities and mechanisms of action of cationic and amphipathic antimicrobial octadecapeptide from rice α‐amylase

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