Enhancement of cytotoxicity of antimicrobial peptide magainin II in tumor cells by bombesin-targeted delivery

Aim： To investigate whether the conjugation of magainin II （MG2）, an antimicrobial peptides （AMPs）, to the tumor-homing peptide bombesin could enhance its cytotoxicity in tumor cells. Methods： A magainin II-bombesin conjugate （MG2B） was constructed by attaching magainin II （MG2） to bombesin at its N...

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Published inActa pharmacologica Sinica Vol. 32; no. 1; pp. 79 - 88
Main Authors Liu, Shan, Yang, Hao, Wan, Lin, Cai, Hua-wei, Li, Sheng-fu, Li, You-ping, Cheng, Jing-qiu, Lu, Xiao-feng
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 01.01.2011
Nature Publishing Group
Subjects
Animals
Antimicrobial Cationic Peptides - administration & dosage
Antimicrobial Cationic Peptides - chemistry
Antimicrobial Cationic Peptides - pharmacology
Antimicrobial Cationic Peptides - therapeutic use
Antineoplastic Agents - administration & dosage
Antineoplastic Agents - chemistry
Antineoplastic Agents - pharmacology
Antineoplastic Agents - therapeutic use
Biomedical and Life Sciences
Biomedicine
Bombesin - chemistry
Bombesin - metabolism
Caspases - metabolism
Cell Death - drug effects
Cell Line, Tumor
Drug Delivery Systems
Female
Humans
Immunology
Internal Medicine
Medical Microbiology
Mice
Mice, Nude
Neoplasms - drug therapy
Original
original-article
Pharmacology/Toxicology
Receptors, Bombesin - metabolism
Vaccine
异种移植
抗肿瘤作用
抗菌多肽
抗菌肽
细胞毒作用
肿瘤细胞
蛙皮素
magainin
targeted cancer therapy
tumor-homing peptide
antimicrobial peptide
bombesin
Online AccessGet full text

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Abstract Aim： To investigate whether the conjugation of magainin II （MG2）, an antimicrobial peptides （AMPs）, to the tumor-homing peptide bombesin could enhance its cytotoxicity in tumor cells. Methods： A magainin II-bombesin conjugate （MG2B） was constructed by attaching magainin II （MG2） to bombesin at its N-terminus. The peptides were synthesized using Fmoc-chemistry. The in vitro cytotoxicity of the peptide in cancer cells was quantitatively deter- mined using the CCK-8 cell counting kit. Moreover, the in vivo antitumor effect of the peptide was determined in tumor xenograft mod- els. Results： The IC5o of MG2B for cancer cells （10-15 pmol/L） was at least 10 times lower than the IC50 of unconjugated MG2 （125 μmol/L）. Moreover, the binding affinity of MG2B for cancer cells was higher than that of unconjugated MG2. in contrast, conjugation to a bombesin analog lacking the receptor-binding domain failed to increase the cytotoxicity of MG2, suggesting that bombesin conjugation enhances the cytotoxicity of MG2 in cancer cells through improved binding. Indeed, MG2B selectively induced cell death in cancer cells in vitro with the IC50 ranging from 10 to 15 pmol/L, which was about 6-10 times lower than the IC5o for normal cells. MG2B （20 mp=/kg per day, intratumorally injected for 5 d） also exhibited antitumor effects in mice bearing MCF-7 tumor grafts. The mean weights of tumor grafts in MG2B- and PBS-treated mice were 0.21±0.05 g and 0.59±0.12 g, respectively. Conclusion： The results suggest that conjugation of AMPs to bombesin might be an alternative approach for targeted cancer therapy.
AbstractList To investigate whether the conjugation of magainin II (MG2), an antimicrobial peptides (AMPs), to the tumor-homing peptide bombesin could enhance its cytotoxicity in tumor cells. A magainin II-bombesin conjugate (MG2B) was constructed by attaching magainin II (MG2) to bombesin at its N-terminus. The peptides were synthesized using Fmoc-chemistry. The in vitro cytotoxicity of the peptide in cancer cells was quantitatively determined using the CCK-8 cell counting kit. Moreover, the in vivo antitumor effect of the peptide was determined in tumor xenograft models. The IC(50) of MG2B for cancer cells (10-15 μmol/L) was at least 10 times lower than the IC(50) of unconjugated MG2 (125 μmol/L). Moreover, the binding affinity of MG2B for cancer cells was higher than that of unconjugated MG2. In contrast, conjugation to a bombesin analog lacking the receptor-binding domain failed to increase the cytotoxicity of MG2, suggesting that bombesin conjugation enhances the cytotoxicity of MG2 in cancer cells through improved binding. Indeed, MG2B selectively induced cell death in cancer cells in vitro with the IC(50) ranging from 10 to 15 μmol/L, which was about 6-10 times lower than the IC(50) for normal cells. MG2B (20 mg/kg per day, intratumorally injected for 5 d) also exhibited antitumor effects in mice bearing MCF-7 tumor grafts. The mean weights of tumor grafts in MG2B- and PBS-treated mice were 0.21±0.05 g and 0.59±0.12 g, respectively. The results suggest that conjugation of AMPs to bombesin might be an alternative approach for targeted cancer therapy.
Aim： To investigate whether the conjugation of magainin II （MG2）, an antimicrobial peptides （AMPs）, to the tumor-homing peptide bombesin could enhance its cytotoxicity in tumor cells. Methods： A magainin II-bombesin conjugate （MG2B） was constructed by attaching magainin II （MG2） to bombesin at its N-terminus. The peptides were synthesized using Fmoc-chemistry. The in vitro cytotoxicity of the peptide in cancer cells was quantitatively deter- mined using the CCK-8 cell counting kit. Moreover, the in vivo antitumor effect of the peptide was determined in tumor xenograft mod- els. Results： The IC5o of MG2B for cancer cells （10-15 pmol/L） was at least 10 times lower than the IC50 of unconjugated MG2 （125 μmol/L）. Moreover, the binding affinity of MG2B for cancer cells was higher than that of unconjugated MG2. in contrast, conjugation to a bombesin analog lacking the receptor-binding domain failed to increase the cytotoxicity of MG2, suggesting that bombesin conjugation enhances the cytotoxicity of MG2 in cancer cells through improved binding. Indeed, MG2B selectively induced cell death in cancer cells in vitro with the IC50 ranging from 10 to 15 pmol/L, which was about 6-10 times lower than the IC5o for normal cells. MG2B （20 mp=/kg per day, intratumorally injected for 5 d） also exhibited antitumor effects in mice bearing MCF-7 tumor grafts. The mean weights of tumor grafts in MG2B- and PBS-treated mice were 0.21±0.05 g and 0.59±0.12 g, respectively. Conclusion： The results suggest that conjugation of AMPs to bombesin might be an alternative approach for targeted cancer therapy.
AIMTo investigate whether the conjugation of magainin II (MG2), an antimicrobial peptides (AMPs), to the tumor-homing peptide bombesin could enhance its cytotoxicity in tumor cells. METHODSA magainin II-bombesin conjugate (MG2B) was constructed by attaching magainin II (MG2) to bombesin at its N-terminus. The peptides were synthesized using Fmoc-chemistry. The in vitro cytotoxicity of the peptide in cancer cells was quantitatively determined using the CCK-8 cell counting kit. Moreover, the in vivo antitumor effect of the peptide was determined in tumor xenograft models. RESULTSThe IC(50) of MG2B for cancer cells (10-15 μmol/L) was at least 10 times lower than the IC(50) of unconjugated MG2 (125 μmol/L). Moreover, the binding affinity of MG2B for cancer cells was higher than that of unconjugated MG2. In contrast, conjugation to a bombesin analog lacking the receptor-binding domain failed to increase the cytotoxicity of MG2, suggesting that bombesin conjugation enhances the cytotoxicity of MG2 in cancer cells through improved binding. Indeed, MG2B selectively induced cell death in cancer cells in vitro with the IC(50) ranging from 10 to 15 μmol/L, which was about 6-10 times lower than the IC(50) for normal cells. MG2B (20 mg/kg per day, intratumorally injected for 5 d) also exhibited antitumor effects in mice bearing MCF-7 tumor grafts. The mean weights of tumor grafts in MG2B- and PBS-treated mice were 0.21±0.05 g and 0.59±0.12 g, respectively. CONCLUSIONThe results suggest that conjugation of AMPs to bombesin might be an alternative approach for targeted cancer therapy.
Aim:To investigate whether the conjugation of magainin II (MG2), an antimicrobial peptides (AMPs), to the tumor-homing peptide bombesin could enhance its cytotoxicity in tumor cells. Methods:A magainin II-bombesin conjugate (MG2B) was constructed by attaching magainin II (MG2) to bombesin at its N-terminus. The peptides were synthesized using Fmoc-chemistry. The in vitro cytotoxicity of the peptide in cancer cells was quantitatively determined using the CCK-8 cell counting kit. Moreover, the in vivo antitumor effect of the peptide was determined in tumor xenograft models. Results:The IC sub(50) of MG2B for cancer cells (10-15 mu mol/L) was at least 10 times lower than the IC sub(50) of unconjugated MG2 (125 mu mol/L). Moreover, the binding affinity of MG2B for cancer cells was higher than that of unconjugated MG2. In contrast, conjugation to a bombesin analog lacking the receptor-binding domain failed to increase the cytotoxicity of MG2, suggesting that bombesin conjugation enhances the cytotoxicity of MG2 in cancer cells through improved binding. Indeed, MG2B selectively induced cell death in cancer cells in vitro with the IC sub(50) ranging from 10 to 15 mu mol/L, which was about 6-10 times lower than the IC sub(50) for normal cells. MG2B (20 mg/kg per day, intratumorally injected for 5 d) also exhibited antitumor effects in mice bearing MCF-7 tumor grafts. The mean weights of tumor grafts in MG2B- and PBS-treated mice were 0.21 plus or minus 0.05 g and 0.59 plus or minus 0.12 g, respectively. Conclusion:The results suggest that conjugation of AMPs to bombesin might be an alternative approach for targeted cancer therapy.
To investigate whether the conjugation of magainin II (MG2), an antimicrobial peptides (AMPs), to the tumor-homing peptide bombesin could enhance its cytotoxicity in tumor cells. A magainin II-bombesin conjugate (MG2B) was constructed by attaching magainin II (MG2) to bombesin at its N-terminus. The peptides were synthesized using Fmoc-chemistry. The in vitro cytotoxicity of the peptide in cancer cells was quantitatively determined using the CCK-8 cell counting kit. Moreover, the in vivo antitumor effect of the peptide was determined in tumor xenograft models. The IC(50) of MG2B for cancer cells (10-15 μmol/L) was at least 10 times lower than the IC(50) of unconjugated MG2 (125 μmol/L). Moreover, the binding affinity of MG2B for cancer cells was higher than that of unconjugated MG2. In contrast, conjugation to a bombesin analog lacking the receptor-binding domain failed to increase the cytotoxicity of MG2, suggesting that bombesin conjugation enhances the cytotoxicity of MG2 in cancer cells through improved binding. Indeed, MG2B selectively induced cell death in cancer cells in vitro with the IC(50) ranging from 10 to 15 μmol/L, which was about 6-10 times lower than the IC(50) for normal cells. MG2B (20 mg/kg per day, intratumorally injected for 5 d) also exhibited antitumor effects in mice bearing MCF-7 tumor grafts. The mean weights of tumor grafts in MG2B- and PBS-treated mice were 0.21±0.05 g and 0.59±0.12 g, respectively. The results suggest that conjugation of AMPs to bombesin might be an alternative approach for targeted cancer therapy.
Aim: To investigate whether the conjugation of magainin II (MG2), an antimicrobial peptides (AMPs), to the tumor-homing peptide bombesin could enhance its cytotoxicity in tumor cells. Methods: A magainin II-bombesin conjugate (MG2B) was constructed by attaching magainin II (MG2) to bombesin at its N-terminus. The peptides were synthesized using Fmoc-chemistry. The in vitro cytotoxicity of the peptide in cancer cells was quantitatively determined using the CCK-8 cell counting kit. Moreover, the in vivo antitumor effect of the peptide was determined in tumor xenograft models. Results: The IC 50 of MG2B for cancer cells (10–15 μmol/L) was at least 10 times lower than the IC 50 of unconjugated MG2 (125 μmol/L). Moreover, the binding affinity of MG2B for cancer cells was higher than that of unconjugated MG2. In contrast, conjugation to a bombesin analog lacking the receptor-binding domain failed to increase the cytotoxicity of MG2, suggesting that bombesin conjugation enhances the cytotoxicity of MG2 in cancer cells through improved binding. Indeed, MG2B selectively induced cell death in cancer cells in vitro with the IC 50 ranging from 10 to 15 μmol/L, which was about 6–10 times lower than the IC 50 for normal cells. MG2B (20 mg/kg per day, intratumorally injected for 5 d) also exhibited antitumor effects in mice bearing MCF-7 tumor grafts. The mean weights of tumor grafts in MG2B- and PBS-treated mice were 0.21±0.05 g and 0.59±0.12 g, respectively. Conclusion: The results suggest that conjugation of AMPs to bombesin might be an alternative approach for targeted cancer therapy.
Author Shan LIU Hao YANG Lin WAN Hua-wei CAI Sheng-fu LI You-ping LI Jing-qiu CHENG Xiao-feng LU
AuthorAffiliation Key Lab of Transplant Engineering and Immunology, Ministry of Health, West China Hospital, Sichuan University, ChenEdu 610041,China
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/21131998$$D View this record in MEDLINE/PubMed
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Issue 1
Keywords magainin
targeted cancer therapy
tumor-homing peptide
antimicrobial peptide
bombesin
Language English
LinkModel DirectLink
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Notes magainin
targeted cancer therapy
tumor-homing peptide
TQ463.54
Q279
targeted cancer therapy; antimicrobial peptide; tumor-homing peptide; bombesin; magainin
antimicrobial peptide
bombesin
31-1347/R
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PublicationTitle Acta pharmacologica Sinica
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Publisher Nature Publishing Group UK
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SSID ssj0032319
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Snippet Aim： To investigate whether the conjugation of magainin II （MG2）, an antimicrobial peptides （AMPs）, to the tumor-homing peptide bombesin could enhance its...
Aim: To investigate whether the conjugation of magainin II (MG2), an antimicrobial peptides (AMPs), to the tumor-homing peptide bombesin could enhance its...
To investigate whether the conjugation of magainin II (MG2), an antimicrobial peptides (AMPs), to the tumor-homing peptide bombesin could enhance its...
AIMTo investigate whether the conjugation of magainin II (MG2), an antimicrobial peptides (AMPs), to the tumor-homing peptide bombesin could enhance its...
Aim:To investigate whether the conjugation of magainin II (MG2), an antimicrobial peptides (AMPs), to the tumor-homing peptide bombesin could enhance its...
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proquest
crossref
pubmed
springer
nature
chongqing
SourceType Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 79
SubjectTerms Animals
Antimicrobial Cationic Peptides - administration & dosage
Antimicrobial Cationic Peptides - chemistry
Antimicrobial Cationic Peptides - pharmacology
Antimicrobial Cationic Peptides - therapeutic use
Antineoplastic Agents - administration & dosage
Antineoplastic Agents - chemistry
Antineoplastic Agents - pharmacology
Antineoplastic Agents - therapeutic use
Biomedical and Life Sciences
Biomedicine
Bombesin - chemistry
Bombesin - metabolism
Caspases - metabolism
Cell Death - drug effects
Cell Line, Tumor
Drug Delivery Systems
Female
Humans
Immunology
Internal Medicine
Medical Microbiology
Mice
Mice, Nude
Neoplasms - drug therapy
Original
original-article
Pharmacology/Toxicology
Receptors, Bombesin - metabolism
Vaccine
异种移植
抗肿瘤作用
抗菌多肽
抗菌肽
细胞毒作用
肿瘤细胞
蛙皮素
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Title Enhancement of cytotoxicity of antimicrobial peptide magainin II in tumor cells by bombesin-targeted delivery
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http://dx.doi.org/10.1038/aps.2010.162
https://link.springer.com/article/10.1038/aps.2010.162
https://www.ncbi.nlm.nih.gov/pubmed/21131998
https://www.proquest.com/docview/822384032
https://search.proquest.com/docview/822708991
https://search.proquest.com/docview/954606488
https://pubmed.ncbi.nlm.nih.gov/PMC4003308
Volume 32
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