Cationic antimicrobial peptide CC34 potential anticancer and apoptotic induction on cancer cells

To evaluate the potential of antimicrobial peptide CC34 for use as therapeutic agents for gastric cancer SGC-7901 and hepatocellular carcinoma HepG-2. In this study, the antibacterial activity and antibacterial mechanism were tested by the minimum inhibitory concentration (MIC) analysis, minimal bac...

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Published inAmino acids Vol. 57; no. 1; p. 28
Main Authors Dong, Liqiang, Li, Yunhe, Zhang, Yaguang, Su, Shi
Format Journal Article
LanguageEnglish
Published Vienna Springer Vienna 24.05.2025
Springer Nature B.V
Springer
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ISSN1438-2199
0939-4451
1438-2199
DOI10.1007/s00726-025-03458-1

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Abstract To evaluate the potential of antimicrobial peptide CC34 for use as therapeutic agents for gastric cancer SGC-7901 and hepatocellular carcinoma HepG-2. In this study, the antibacterial activity and antibacterial mechanism were tested by the minimum inhibitory concentration (MIC) analysis, minimal bactericidal concentration (MBC) analysis, bacterial biofilm and NaCl permeability assays. Then, we assessed the hemolytic activity and cytotoxicity of CC34 for red blood cells and cancer cells, respectively. Apoptosis assay, cell cycle analysis, determination of intracellular ROS, western blot analysis caspase activity assay and ATP assay were further performed to investigate the mechanism of CC34 affected cancer cells. The novel peptide could inhibit Gram-negative and Gram-positive bacteria, with low hemolytic activity against mouse and chicken erythrocytes. Moreover, CC34 exhibited higher inhibitory activity against biofilm formation. In addition, our data showed that CC34 significantly suppressed cell proliferation, in a dose dependent manner. CC34 induced apoptosis, induced reactive oxygen species (ROS) generation, inhibited B-cell lymphoma-2 (Bcl-2) expression, increase B-cell lymphoma protein 2 associated X protein (Bax) expression, release of cytochrome c (Cyt C), promoted caspase-3 and − 9 activities and reduced cellular ATP levels in cancer cells. Our results indicate that CC34 with antimicrobial activity have a highly potent ability to induced apoptosis via mitochondrial-mediated apoptotic pathway in cancer cells.
AbstractList To evaluate the potential of antimicrobial peptide CC34 for use as therapeutic agents for gastric cancer SGC-7901 and hepatocellular carcinoma HepG-2. In this study, the antibacterial activity and antibacterial mechanism were tested by the minimum inhibitory concentration (MIC) analysis, minimal bactericidal concentration (MBC) analysis, bacterial biofilm and NaCl permeability assays. Then, we assessed the hemolytic activity and cytotoxicity of CC34 for red blood cells and cancer cells, respectively. Apoptosis assay, cell cycle analysis, determination of intracellular ROS, western blot analysis caspase activity assay and ATP assay were further performed to investigate the mechanism of CC34 affected cancer cells. The novel peptide could inhibit Gram-negative and Gram-positive bacteria, with low hemolytic activity against mouse and chicken erythrocytes. Moreover, CC34 exhibited higher inhibitory activity against biofilm formation. In addition, our data showed that CC34 significantly suppressed cell proliferation, in a dose dependent manner. CC34 induced apoptosis, induced reactive oxygen species (ROS) generation, inhibited B-cell lymphoma-2 (Bcl-2) expression, increase B-cell lymphoma protein 2 associated X protein (Bax) expression, release of cytochrome c (Cyt C), promoted caspase-3 and − 9 activities and reduced cellular ATP levels in cancer cells. Our results indicate that CC34 with antimicrobial activity have a highly potent ability to induced apoptosis via mitochondrial-mediated apoptotic pathway in cancer cells.
Abstract To evaluate the potential of antimicrobial peptide CC34 for use as therapeutic agents for gastric cancer SGC-7901 and hepatocellular carcinoma HepG-2. In this study, the antibacterial activity and antibacterial mechanism were tested by the minimum inhibitory concentration (MIC) analysis, minimal bactericidal concentration (MBC) analysis, bacterial biofilm and NaCl permeability assays. Then, we assessed the hemolytic activity and cytotoxicity of CC34 for red blood cells and cancer cells, respectively. Apoptosis assay, cell cycle analysis, determination of intracellular ROS, western blot analysis caspase activity assay and ATP assay were further performed to investigate the mechanism of CC34 affected cancer cells. The novel peptide could inhibit Gram-negative and Gram-positive bacteria, with low hemolytic activity against mouse and chicken erythrocytes. Moreover, CC34 exhibited higher inhibitory activity against biofilm formation. In addition, our data showed that CC34 significantly suppressed cell proliferation, in a dose dependent manner. CC34 induced apoptosis, induced reactive oxygen species (ROS) generation, inhibited B-cell lymphoma-2 (Bcl-2) expression, increase B-cell lymphoma protein 2 associated X protein (Bax) expression, release of cytochrome c (Cyt C), promoted caspase-3 and − 9 activities and reduced cellular ATP levels in cancer cells. Our results indicate that CC34 with antimicrobial activity have a highly potent ability to induced apoptosis via mitochondrial-mediated apoptotic pathway in cancer cells.
To evaluate the potential of antimicrobial peptide CC34 for use as therapeutic agents for gastric cancer SGC-7901 and hepatocellular carcinoma HepG-2. In this study, the antibacterial activity and antibacterial mechanism were tested by the minimum inhibitory concentration (MIC) analysis, minimal bactericidal concentration (MBC) analysis, bacterial biofilm and NaCl permeability assays. Then, we assessed the hemolytic activity and cytotoxicity of CC34 for red blood cells and cancer cells, respectively. Apoptosis assay, cell cycle analysis, determination of intracellular ROS, western blot analysis caspase activity assay and ATP assay were further performed to investigate the mechanism of CC34 affected cancer cells. The novel peptide could inhibit Gram-negative and Gram-positive bacteria, with low hemolytic activity against mouse and chicken erythrocytes. Moreover, CC34 exhibited higher inhibitory activity against biofilm formation. In addition, our data showed that CC34 significantly suppressed cell proliferation, in a dose dependent manner. CC34 induced apoptosis, induced reactive oxygen species (ROS) generation, inhibited B-cell lymphoma-2 (Bcl-2) expression, increase B-cell lymphoma protein 2 associated X protein (Bax) expression, release of cytochrome c (Cyt C), promoted caspase-3 and - 9 activities and reduced cellular ATP levels in cancer cells. Our results indicate that CC34 with antimicrobial activity have a highly potent ability to induced apoptosis via mitochondrial-mediated apoptotic pathway in cancer cells.To evaluate the potential of antimicrobial peptide CC34 for use as therapeutic agents for gastric cancer SGC-7901 and hepatocellular carcinoma HepG-2. In this study, the antibacterial activity and antibacterial mechanism were tested by the minimum inhibitory concentration (MIC) analysis, minimal bactericidal concentration (MBC) analysis, bacterial biofilm and NaCl permeability assays. Then, we assessed the hemolytic activity and cytotoxicity of CC34 for red blood cells and cancer cells, respectively. Apoptosis assay, cell cycle analysis, determination of intracellular ROS, western blot analysis caspase activity assay and ATP assay were further performed to investigate the mechanism of CC34 affected cancer cells. The novel peptide could inhibit Gram-negative and Gram-positive bacteria, with low hemolytic activity against mouse and chicken erythrocytes. Moreover, CC34 exhibited higher inhibitory activity against biofilm formation. In addition, our data showed that CC34 significantly suppressed cell proliferation, in a dose dependent manner. CC34 induced apoptosis, induced reactive oxygen species (ROS) generation, inhibited B-cell lymphoma-2 (Bcl-2) expression, increase B-cell lymphoma protein 2 associated X protein (Bax) expression, release of cytochrome c (Cyt C), promoted caspase-3 and - 9 activities and reduced cellular ATP levels in cancer cells. Our results indicate that CC34 with antimicrobial activity have a highly potent ability to induced apoptosis via mitochondrial-mediated apoptotic pathway in cancer cells.
To evaluate the potential of antimicrobial peptide CC34 for use as therapeutic agents for gastric cancer SGC-7901 and hepatocellular carcinoma HepG-2. In this study, the antibacterial activity and antibacterial mechanism were tested by the minimum inhibitory concentration (MIC) analysis, minimal bactericidal concentration (MBC) analysis, bacterial biofilm and NaCl permeability assays. Then, we assessed the hemolytic activity and cytotoxicity of CC34 for red blood cells and cancer cells, respectively. Apoptosis assay, cell cycle analysis, determination of intracellular ROS, western blot analysis caspase activity assay and ATP assay were further performed to investigate the mechanism of CC34 affected cancer cells. The novel peptide could inhibit Gram-negative and Gram-positive bacteria, with low hemolytic activity against mouse and chicken erythrocytes. Moreover, CC34 exhibited higher inhibitory activity against biofilm formation. In addition, our data showed that CC34 significantly suppressed cell proliferation, in a dose dependent manner. CC34 induced apoptosis, induced reactive oxygen species (ROS) generation, inhibited B-cell lymphoma-2 (Bcl-2) expression, increase B-cell lymphoma protein 2 associated X protein (Bax) expression, release of cytochrome c (Cyt C), promoted caspase-3 and - 9 activities and reduced cellular ATP levels in cancer cells. Our results indicate that CC34 with antimicrobial activity have a highly potent ability to induced apoptosis via mitochondrial-mediated apoptotic pathway in cancer cells.
ArticleNumber 28
Author Li, Yunhe
Dong, Liqiang
Zhang, Yaguang
Su, Shi
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Cites_doi 10.1186/s12866-016-0904-3
10.1007/s10534-017-0060-8
10.1042/bsr20180710
10.1073/pnas.97.16.8856
10.18632/oncotarget.16743
10.1128/aem.02769-17
10.3390/microorganisms9061249
10.3390/ijms21176216
10.1128/aac.46.11.3585-3590
10.3892/ijo.2015.2933
10.2174/092986712801661004
10.3390/md18080380
10.1007/s10930-016-9662-1
10.1016/j.peptides.2011.11.002
10.1016/0008-8749(91)90136-y
10.1016/j.jgar.2018.12.004
10.1002/psc.1144
10.1016/j.fitote.2015.12.021
10.1016/j.micpath.2018.04.008
10.3748/wjg.v8.i6.1053
10.1007/s11274-015-1986-z
10.2174/1573406415666190222141905
10.1016/j.peptides.2010.05.008
10.2174/0929866524666170202153501
10.1111/cbdd.12927
10.1038/s41522-020-0116-3
10.1038/s41586-020-2761-3
10.3389/fcimb.2016.00194
10.1016/j.ejmech.2019.06.080
10.21873/invivo.11206
10.3892/or.2020.7517
10.3389/fmicb.2021.661195
10.3892/ol.2016.4601
10.1021/acs.jmedchem.6b00922
10.1002/ptr.3259
10.3390/pharmaceutics12111045
10.1186/s12885-016-3003-9
10.1016/j.bbamem.2007.11.008
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Issue 1
Keywords Caspase
Antibacterial
Anticancer
ROS
Apoptosis
Language English
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References J Koehbach (3458_CR13) 2021; 9
Y Tülüce (3458_CR36) 2017; 30
M Krishnan (3458_CR14) 2020; 21
M Margit (3458_CR21) 2017; 6
L Xia (3458_CR38) 2016; 12
M Kalsy (3458_CR12) 2020; 6
ML Olson (3458_CR26) 2018; 84
JF Gera (3458_CR8) 1991; 138
M Burdukiewicz (3458_CR3) 2020; 12
X Chen (3458_CR5) 2018; 38
T Theansungnoen (3458_CR35) 2016; 35
G Bocchinfuso (3458_CR1) 2009; 15
K Kuroda (3458_CR15) 2017; 17
Z Ma (3458_CR20) 2016; 59
J Slaninová (3458_CR31) 2012; 33
3458_CR34
3458_CR10
3458_CR32
RJ Boohaker (3458_CR2) 2012; 19
MA Esmaeili (3458_CR7) 2016; 109
H Memariani (3458_CR24) 2018; 119
V Maselli (3458_CR22) 2020; 18
GL Ouyang (3458_CR28) 2002; 8
A Sahoo (3458_CR29) 2021; 12
Q Li (3458_CR17) 2020; 586
JM Cerón (3458_CR4) 2010; 31
J Li (3458_CR16) 2020; 43
N Losuwannarak (3458_CR19) 2018; 32
C Liu (3458_CR18) 2011; 25
YL Wu (3458_CR37) 2015; 46
B Deslouches (3458_CR6) 2017; 8
E Mataracı Kara (3458_CR23) 2019; 17
L Otvos (3458_CR27) 2017; 24
3458_CR40
F Hu (3458_CR11) 2016; 16
P Strzelecka (3458_CR33) 2017; 90
D Zhang (3458_CR39) 2019; 26
EN Grafskaia (3458_CR9) 2019; 180
3458_CR25
N Shagaghi (3458_CR30) 2016; 32
References_xml – volume: 16
  start-page: 287
  issue: 1
  year: 2016
  ident: 3458_CR11
  publication-title: BMC Microbiol
  doi: 10.1186/s12866-016-0904-3
– volume: 30
  start-page: 933
  issue: 6
  year: 2017
  ident: 3458_CR36
  publication-title: Biometals
  doi: 10.1007/s10534-017-0060-8
– volume: 38
  start-page: BSR20180710
  issue: 6
  year: 2018
  ident: 3458_CR5
  publication-title: Biosci Rep
  doi: 10.1042/bsr20180710
– ident: 3458_CR34
– ident: 3458_CR10
  doi: 10.1073/pnas.97.16.8856
– volume: 8
  start-page: 46635
  issue: 28
  year: 2017
  ident: 3458_CR6
  publication-title: Oncotarget
  doi: 10.18632/oncotarget.16743
– volume: 84
  start-page: e02769
  issue: 8
  year: 2018
  ident: 3458_CR26
  publication-title: Appl Environ Microbiol
  doi: 10.1128/aem.02769-17
– volume: 9
  start-page: 1249
  issue: 6
  year: 2021
  ident: 3458_CR13
  publication-title: Microorganisms
  doi: 10.3390/microorganisms9061249
– volume: 21
  start-page: 6216
  issue: 17
  year: 2020
  ident: 3458_CR14
  publication-title: Int J Mol Sci
  doi: 10.3390/ijms21176216
– ident: 3458_CR32
  doi: 10.1128/aac.46.11.3585-3590
– volume: 46
  start-page: 2181
  issue: 5
  year: 2015
  ident: 3458_CR37
  publication-title: Int J Oncol
  doi: 10.3892/ijo.2015.2933
– volume: 19
  start-page: 3794
  issue: 22
  year: 2012
  ident: 3458_CR2
  publication-title: Curr Med Chem
  doi: 10.2174/092986712801661004
– volume: 18
  start-page: 380
  issue: 8
  year: 2020
  ident: 3458_CR22
  publication-title: Mar Drugs
  doi: 10.3390/md18080380
– volume: 35
  start-page: 202
  issue: 3
  year: 2016
  ident: 3458_CR35
  publication-title: Protein J
  doi: 10.1007/s10930-016-9662-1
– volume: 33
  start-page: 18
  issue: 1
  year: 2012
  ident: 3458_CR31
  publication-title: Peptides
  doi: 10.1016/j.peptides.2011.11.002
– volume: 138
  start-page: 108
  issue: 1
  year: 1991
  ident: 3458_CR8
  publication-title: Cell Immunol
  doi: 10.1016/0008-8749(91)90136-y
– volume: 17
  start-page: 137
  year: 2019
  ident: 3458_CR23
  publication-title: J Glob Antimicrob Resist
  doi: 10.1016/j.jgar.2018.12.004
– volume: 15
  start-page: 550
  issue: 9
  year: 2009
  ident: 3458_CR1
  publication-title: J Pept Sci
  doi: 10.1002/psc.1144
– volume: 109
  start-page: 162
  year: 2016
  ident: 3458_CR7
  publication-title: Fitoterapia
  doi: 10.1016/j.fitote.2015.12.021
– volume: 119
  start-page: 72
  year: 2018
  ident: 3458_CR24
  publication-title: Microb Pathog
  doi: 10.1016/j.micpath.2018.04.008
– volume: 8
  start-page: 1053
  issue: 6
  year: 2002
  ident: 3458_CR28
  publication-title: World J Gastroenterol
  doi: 10.3748/wjg.v8.i6.1053
– volume: 32
  start-page: 31
  issue: 2
  year: 2016
  ident: 3458_CR30
  publication-title: World J Microbiol Biotechnol
  doi: 10.1007/s11274-015-1986-z
– volume: 26
  start-page: 564
  issue: 8
  year: 2019
  ident: 3458_CR39
  publication-title: Protein Pept Lett
  doi: 10.2174/1573406415666190222141905
– volume: 31
  start-page: 1494
  issue: 8
  year: 2010
  ident: 3458_CR4
  publication-title: Peptides
  doi: 10.1016/j.peptides.2010.05.008
– volume: 24
  start-page: 879
  issue: 10
  year: 2017
  ident: 3458_CR27
  publication-title: Protein Pept Lett
  doi: 10.2174/0929866524666170202153501
– volume: 90
  start-page: 52
  issue: 1
  year: 2017
  ident: 3458_CR33
  publication-title: Chem Biol Drug Des
  doi: 10.1111/cbdd.12927
– volume: 6
  start-page: 6
  issue: 1
  year: 2020
  ident: 3458_CR12
  publication-title: NPJ Biofilms Microbiomes
  doi: 10.1038/s41522-020-0116-3
– volume: 586
  start-page: 145
  issue: 7827
  year: 2020
  ident: 3458_CR17
  publication-title: Nature
  doi: 10.1038/s41586-020-2761-3
– ident: 3458_CR25
– volume: 6
  start-page: 194
  year: 2017
  ident: 3458_CR21
  publication-title: Front Cell Infect Microbiol
  doi: 10.3389/fcimb.2016.00194
– volume: 180
  start-page: 143
  year: 2019
  ident: 3458_CR9
  publication-title: Eur J Med Chem
  doi: 10.1016/j.ejmech.2019.06.080
– volume: 32
  start-page: 71
  issue: 1
  year: 2018
  ident: 3458_CR19
  publication-title: Vivo
  doi: 10.21873/invivo.11206
– volume: 43
  start-page: 1516
  issue: 5
  year: 2020
  ident: 3458_CR16
  publication-title: Oncol Rep
  doi: 10.3892/or.2020.7517
– volume: 12
  start-page: 661195
  year: 2021
  ident: 3458_CR29
  publication-title: Front Microbiol
  doi: 10.3389/fmicb.2021.661195
– volume: 12
  start-page: 57
  issue: 1
  year: 2016
  ident: 3458_CR38
  publication-title: Oncol Lett
  doi: 10.3892/ol.2016.4601
– volume: 59
  start-page: 10946
  issue: 24
  year: 2016
  ident: 3458_CR20
  publication-title: J Med Chem
  doi: 10.1021/acs.jmedchem.6b00922
– volume: 25
  start-page: 277
  issue: 2
  year: 2011
  ident: 3458_CR18
  publication-title: Phytother Res
  doi: 10.1002/ptr.3259
– volume: 12
  start-page: 1045
  issue: 11
  year: 2020
  ident: 3458_CR3
  publication-title: Pharmaceutics
  doi: 10.3390/pharmaceutics12111045
– volume: 17
  start-page: 33
  issue: 1
  year: 2017
  ident: 3458_CR15
  publication-title: BMC Cancer
  doi: 10.1186/s12885-016-3003-9
– ident: 3458_CR40
  doi: 10.1016/j.bbamem.2007.11.008
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Snippet To evaluate the potential of antimicrobial peptide CC34 for use as therapeutic agents for gastric cancer SGC-7901 and hepatocellular carcinoma HepG-2. In this...
Abstract To evaluate the potential of antimicrobial peptide CC34 for use as therapeutic agents for gastric cancer SGC-7901 and hepatocellular carcinoma HepG-2....
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SubjectTerms Adenosine Triphosphate - metabolism
Analytical Chemistry
Animals
Anti-Bacterial Agents - pharmacology
Antibacterial
Antibacterial activity
antibacterial properties
Anticancer
Antiinfectives and antibacterials
Antimicrobial activity
Antimicrobial agents
Antimicrobial Cationic Peptides - chemistry
Antimicrobial Cationic Peptides - pharmacology
Antimicrobial peptides
Antineoplastic Agents - chemistry
Antineoplastic Agents - pharmacology
Apoptosis
Apoptosis - drug effects
Assaying
B-cell lymphoma
B-lymphocytes
Bacteria
Bcl-2 protein
Bcl-x protein
Biochemical Engineering
Biochemistry
biofilm
Biofilms
Biofilms - drug effects
Biomedical and Life Sciences
Cancer
Caspase
Caspase-3
Cell cycle
Cell Line, Tumor
Cell proliferation
Cell Proliferation - drug effects
chickens
Cytochrome c
Cytotoxicity
dose response
Erythrocytes
Erythrocytes - drug effects
Gastric cancer
Gram-negative bacteria
Gram-positive bacteria
hemolysis
Hep G2 Cells
Hepatocellular carcinoma
hepatoma
Humans
Life Sciences
Lymphocytes B
Lymphoma
Mice
Microbial Sensitivity Tests
Minimum inhibitory concentration
Neurobiology
Original
Original Article
Peptides
permeability
Pharmacology
Proteins
Proteomics
Reactive oxygen species
Reactive Oxygen Species - metabolism
ROS
Sodium chloride
stomach neoplasms
therapeutics
Western blotting
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Title Cationic antimicrobial peptide CC34 potential anticancer and apoptotic induction on cancer cells
URI https://link.springer.com/article/10.1007/s00726-025-03458-1
https://www.ncbi.nlm.nih.gov/pubmed/40413361
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Volume 57
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