Novel Hybrid Peptide Cathelicidin 2 (1-13)-Thymopentin (TP5) and Its Derived Peptides with Effective Antibacterial, Antibiofilm, and Anti-Adhesion Activities
The increasing numbers of infections caused by multidrug-resistant (MDR) pathogens highlight the urgent need for new alternatives to conventional antibiotics. Antimicrobial peptides have the potential to be promising alternatives to antibiotics because of their effective bactericidal activity and hi...
Guardado en:
| Autores principales: | , , , , , , , , , , , , , , , , , |
|---|---|
| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
MDPI AG
2021
|
| Materias: | |
| Acceso en línea: | https://doaj.org/article/7b81f3d94b544d1381d994fda718f29f |
| Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
| id |
oai:doaj.org-article:7b81f3d94b544d1381d994fda718f29f |
|---|---|
| record_format |
dspace |
| spelling |
oai:doaj.org-article:7b81f3d94b544d1381d994fda718f29f2021-11-11T17:08:46ZNovel Hybrid Peptide Cathelicidin 2 (1-13)-Thymopentin (TP5) and Its Derived Peptides with Effective Antibacterial, Antibiofilm, and Anti-Adhesion Activities10.3390/ijms2221116811422-00671661-6596https://doaj.org/article/7b81f3d94b544d1381d994fda718f29f2021-10-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/21/11681https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067The increasing numbers of infections caused by multidrug-resistant (MDR) pathogens highlight the urgent need for new alternatives to conventional antibiotics. Antimicrobial peptides have the potential to be promising alternatives to antibiotics because of their effective bactericidal activity and highly selective toxicity. The present study was conducted to investigate the antibacterial, antibiofilm, and anti-adhesion activities of different CTP peptides (CTP: the original hybrid peptide cathelicidin 2 (1-13)-thymopentin (TP5); CTP-NH<sub>2</sub>: C-terminal amidated derivative of cathelicidin 2 (1-13)-TP5; CTPQ: glutamine added at the C-terminus of cathelicidin 2 (1-13)-TP5) by determining the minimal inhibitory concentrations (MICs), minimal bactericidal concentrations (MBCs), propidium iodide uptake, and analysis by scanning electron microscopy, transmission electron microscopy, and confocal laser scanning microscopy). The results showed that CTPs had broad-spectrum antibacterial activity against different gram-positive and gram-negative bacteria, with MICs against the tested strains varying from 2 to 64 μg/mL. CTPs at the MBC (2 × MIC 64 μg/mL) showed strong bactericidal effects on a standard methicillin-resistant <i>Staphylococcus aureus</i> strain ATCC 43300 after co-incubation for 6 h through disruption of the bacterial membrane. In addition, CTPs at 2 × MIC also displayed effective inhibition activity of several <i>S. aureus</i> strains with a 40–90% decrease in biofilm formation by killing the bacteria embedded in the biofilms. CTPs had low cytotoxicity on the intestinal porcine epithelial cell line (IPEC-J2) and could significantly decrease the rate of adhesion of <i>S. aureus</i> ATCC 43300 on IPEC-J2 cells. The current study proved that CTPs have effective antibacterial, antibiofilm, and anti-adhesion activities. Overall, this study contributes to our understanding of the possible antibacterial and antibiofilm mechanisms of CTPs, which might be an effective anti-MDR drug candidate.He-Nan GuoYu-Cui TongHui-Li WangJing ZhangZhong-Xuan LiZaheer AbbasTian-Tian YangMeng-Yao LiuPei-Yao ChenZheng-Chang HuaXiao-Na YanQiang ChengMarhaba AhmatJun-Yong WangLu-Lu ZhangXu-Biao WeiXiu-Dong LiaoRi-Jun ZhangMDPI AGarticleantimicrobial peptidescathelicidin 2 (1-13)-thymopentin (TP5)multidrug resistance<i>Staphylococcus aureus</i>antibacterialantibiofilmBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 11681, p 11681 (2021) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
antimicrobial peptides cathelicidin 2 (1-13)-thymopentin (TP5) multidrug resistance <i>Staphylococcus aureus</i> antibacterial antibiofilm Biology (General) QH301-705.5 Chemistry QD1-999 |
| spellingShingle |
antimicrobial peptides cathelicidin 2 (1-13)-thymopentin (TP5) multidrug resistance <i>Staphylococcus aureus</i> antibacterial antibiofilm Biology (General) QH301-705.5 Chemistry QD1-999 He-Nan Guo Yu-Cui Tong Hui-Li Wang Jing Zhang Zhong-Xuan Li Zaheer Abbas Tian-Tian Yang Meng-Yao Liu Pei-Yao Chen Zheng-Chang Hua Xiao-Na Yan Qiang Cheng Marhaba Ahmat Jun-Yong Wang Lu-Lu Zhang Xu-Biao Wei Xiu-Dong Liao Ri-Jun Zhang Novel Hybrid Peptide Cathelicidin 2 (1-13)-Thymopentin (TP5) and Its Derived Peptides with Effective Antibacterial, Antibiofilm, and Anti-Adhesion Activities |
| description |
The increasing numbers of infections caused by multidrug-resistant (MDR) pathogens highlight the urgent need for new alternatives to conventional antibiotics. Antimicrobial peptides have the potential to be promising alternatives to antibiotics because of their effective bactericidal activity and highly selective toxicity. The present study was conducted to investigate the antibacterial, antibiofilm, and anti-adhesion activities of different CTP peptides (CTP: the original hybrid peptide cathelicidin 2 (1-13)-thymopentin (TP5); CTP-NH<sub>2</sub>: C-terminal amidated derivative of cathelicidin 2 (1-13)-TP5; CTPQ: glutamine added at the C-terminus of cathelicidin 2 (1-13)-TP5) by determining the minimal inhibitory concentrations (MICs), minimal bactericidal concentrations (MBCs), propidium iodide uptake, and analysis by scanning electron microscopy, transmission electron microscopy, and confocal laser scanning microscopy). The results showed that CTPs had broad-spectrum antibacterial activity against different gram-positive and gram-negative bacteria, with MICs against the tested strains varying from 2 to 64 μg/mL. CTPs at the MBC (2 × MIC 64 μg/mL) showed strong bactericidal effects on a standard methicillin-resistant <i>Staphylococcus aureus</i> strain ATCC 43300 after co-incubation for 6 h through disruption of the bacterial membrane. In addition, CTPs at 2 × MIC also displayed effective inhibition activity of several <i>S. aureus</i> strains with a 40–90% decrease in biofilm formation by killing the bacteria embedded in the biofilms. CTPs had low cytotoxicity on the intestinal porcine epithelial cell line (IPEC-J2) and could significantly decrease the rate of adhesion of <i>S. aureus</i> ATCC 43300 on IPEC-J2 cells. The current study proved that CTPs have effective antibacterial, antibiofilm, and anti-adhesion activities. Overall, this study contributes to our understanding of the possible antibacterial and antibiofilm mechanisms of CTPs, which might be an effective anti-MDR drug candidate. |
| format |
article |
| author |
He-Nan Guo Yu-Cui Tong Hui-Li Wang Jing Zhang Zhong-Xuan Li Zaheer Abbas Tian-Tian Yang Meng-Yao Liu Pei-Yao Chen Zheng-Chang Hua Xiao-Na Yan Qiang Cheng Marhaba Ahmat Jun-Yong Wang Lu-Lu Zhang Xu-Biao Wei Xiu-Dong Liao Ri-Jun Zhang |
| author_facet |
He-Nan Guo Yu-Cui Tong Hui-Li Wang Jing Zhang Zhong-Xuan Li Zaheer Abbas Tian-Tian Yang Meng-Yao Liu Pei-Yao Chen Zheng-Chang Hua Xiao-Na Yan Qiang Cheng Marhaba Ahmat Jun-Yong Wang Lu-Lu Zhang Xu-Biao Wei Xiu-Dong Liao Ri-Jun Zhang |
| author_sort |
He-Nan Guo |
| title |
Novel Hybrid Peptide Cathelicidin 2 (1-13)-Thymopentin (TP5) and Its Derived Peptides with Effective Antibacterial, Antibiofilm, and Anti-Adhesion Activities |
| title_short |
Novel Hybrid Peptide Cathelicidin 2 (1-13)-Thymopentin (TP5) and Its Derived Peptides with Effective Antibacterial, Antibiofilm, and Anti-Adhesion Activities |
| title_full |
Novel Hybrid Peptide Cathelicidin 2 (1-13)-Thymopentin (TP5) and Its Derived Peptides with Effective Antibacterial, Antibiofilm, and Anti-Adhesion Activities |
| title_fullStr |
Novel Hybrid Peptide Cathelicidin 2 (1-13)-Thymopentin (TP5) and Its Derived Peptides with Effective Antibacterial, Antibiofilm, and Anti-Adhesion Activities |
| title_full_unstemmed |
Novel Hybrid Peptide Cathelicidin 2 (1-13)-Thymopentin (TP5) and Its Derived Peptides with Effective Antibacterial, Antibiofilm, and Anti-Adhesion Activities |
| title_sort |
novel hybrid peptide cathelicidin 2 (1-13)-thymopentin (tp5) and its derived peptides with effective antibacterial, antibiofilm, and anti-adhesion activities |
| publisher |
MDPI AG |
| publishDate |
2021 |
| url |
https://doaj.org/article/7b81f3d94b544d1381d994fda718f29f |
| work_keys_str_mv |
AT henanguo novelhybridpeptidecathelicidin2113thymopentintp5anditsderivedpeptideswitheffectiveantibacterialantibiofilmandantiadhesionactivities AT yucuitong novelhybridpeptidecathelicidin2113thymopentintp5anditsderivedpeptideswitheffectiveantibacterialantibiofilmandantiadhesionactivities AT huiliwang novelhybridpeptidecathelicidin2113thymopentintp5anditsderivedpeptideswitheffectiveantibacterialantibiofilmandantiadhesionactivities AT jingzhang novelhybridpeptidecathelicidin2113thymopentintp5anditsderivedpeptideswitheffectiveantibacterialantibiofilmandantiadhesionactivities AT zhongxuanli novelhybridpeptidecathelicidin2113thymopentintp5anditsderivedpeptideswitheffectiveantibacterialantibiofilmandantiadhesionactivities AT zaheerabbas novelhybridpeptidecathelicidin2113thymopentintp5anditsderivedpeptideswitheffectiveantibacterialantibiofilmandantiadhesionactivities AT tiantianyang novelhybridpeptidecathelicidin2113thymopentintp5anditsderivedpeptideswitheffectiveantibacterialantibiofilmandantiadhesionactivities AT mengyaoliu novelhybridpeptidecathelicidin2113thymopentintp5anditsderivedpeptideswitheffectiveantibacterialantibiofilmandantiadhesionactivities AT peiyaochen novelhybridpeptidecathelicidin2113thymopentintp5anditsderivedpeptideswitheffectiveantibacterialantibiofilmandantiadhesionactivities AT zhengchanghua novelhybridpeptidecathelicidin2113thymopentintp5anditsderivedpeptideswitheffectiveantibacterialantibiofilmandantiadhesionactivities AT xiaonayan novelhybridpeptidecathelicidin2113thymopentintp5anditsderivedpeptideswitheffectiveantibacterialantibiofilmandantiadhesionactivities AT qiangcheng novelhybridpeptidecathelicidin2113thymopentintp5anditsderivedpeptideswitheffectiveantibacterialantibiofilmandantiadhesionactivities AT marhabaahmat novelhybridpeptidecathelicidin2113thymopentintp5anditsderivedpeptideswitheffectiveantibacterialantibiofilmandantiadhesionactivities AT junyongwang novelhybridpeptidecathelicidin2113thymopentintp5anditsderivedpeptideswitheffectiveantibacterialantibiofilmandantiadhesionactivities AT luluzhang novelhybridpeptidecathelicidin2113thymopentintp5anditsderivedpeptideswitheffectiveantibacterialantibiofilmandantiadhesionactivities AT xubiaowei novelhybridpeptidecathelicidin2113thymopentintp5anditsderivedpeptideswitheffectiveantibacterialantibiofilmandantiadhesionactivities AT xiudongliao novelhybridpeptidecathelicidin2113thymopentintp5anditsderivedpeptideswitheffectiveantibacterialantibiofilmandantiadhesionactivities AT rijunzhang novelhybridpeptidecathelicidin2113thymopentintp5anditsderivedpeptideswitheffectiveantibacterialantibiofilmandantiadhesionactivities |
| _version_ |
1718432185777651712 |