Eintrag weiter verarbeiten
Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria
Gespeichert in:
| Zeitschriftentitel: | International Journal of Molecular Sciences |
|---|---|
| Personen und Körperschaften: | , , , , , , , |
| In: | International Journal of Molecular Sciences, 20, 2019, 16, S. 3954 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
MDPI AG
|
| Schlagwörter: |
| author_facet |
Dong, Na Wang, Chensi Zhang, Tingting Zhang, Lei Xue, Chenyu Feng, Xinjun Bi, Chongpeng Shan, Anshan Dong, Na Wang, Chensi Zhang, Tingting Zhang, Lei Xue, Chenyu Feng, Xinjun Bi, Chongpeng Shan, Anshan |
|---|---|
| author |
Dong, Na Wang, Chensi Zhang, Tingting Zhang, Lei Xue, Chenyu Feng, Xinjun Bi, Chongpeng Shan, Anshan |
| spellingShingle |
Dong, Na Wang, Chensi Zhang, Tingting Zhang, Lei Xue, Chenyu Feng, Xinjun Bi, Chongpeng Shan, Anshan International Journal of Molecular Sciences Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria Inorganic Chemistry Organic Chemistry Physical and Theoretical Chemistry Computer Science Applications Spectroscopy Molecular Biology General Medicine Catalysis |
| author_sort |
dong, na |
| spelling |
Dong, Na Wang, Chensi Zhang, Tingting Zhang, Lei Xue, Chenyu Feng, Xinjun Bi, Chongpeng Shan, Anshan 1422-0067 MDPI AG Inorganic Chemistry Organic Chemistry Physical and Theoretical Chemistry Computer Science Applications Spectroscopy Molecular Biology General Medicine Catalysis http://dx.doi.org/10.3390/ijms20163954 <jats:p>Antibacterial peptides (APMs) are a new type of antibacterial substance. The relationship between their structure and function remains indistinct; in particular, there is a lack of a definitive and fixed template for designing new antimicrobial peptides. Previous studies have shown that porcine Protegrin-1 (PG-1) exhibits considerable antimicrobial activity and cytotoxicity. In this study, to reduce cytotoxicity and increase cell selectivity, we designed histidine-rich peptides based on the sequence template RR(XY)2XDPGX(YX)2RR-NH2, where X represents I, W, V, and F. The results showed that the peptides form more β-hairpin structures in a lipid-rich environment that mimics cell membranes. Among them, the antimicrobial peptide HV2 showed strong antibacterial activity against Gram-negative strains and almost no toxicity to normal cells. The results of our analysis of its antibacterial mechanism showed that peptide HV2 acts on the bacterial cell membrane to increase its permeability, resulting in cell membrane disruption and death. Furthermore, peptide HV2 inhibited bacterial movement in a concentration-dependent manner and had a more robust anti-inflammatory effect by inhibiting the production of TNF-α. In summary, peptide HV2 exhibits high bactericidal activity and cell selectivity, making it a promising candidate for future use as an antibiotic.</jats:p> Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria International Journal of Molecular Sciences |
| doi_str_mv |
10.3390/ijms20163954 |
| facet_avail |
Online Free |
| finc_class_facet |
Physik Informatik Biologie Chemie und Pharmazie |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMzM5MC9pam1zMjAxNjM5NTQ |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMzM5MC9pam1zMjAxNjM5NTQ |
| institution |
DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 DE-Gla1 DE-Zi4 DE-15 DE-Pl11 DE-Rs1 DE-105 DE-14 |
| imprint |
MDPI AG, 2019 |
| imprint_str_mv |
MDPI AG, 2019 |
| issn |
1422-0067 |
| issn_str_mv |
1422-0067 |
| language |
English |
| mega_collection |
MDPI AG (CrossRef) |
| match_str |
dong2019bioactivityandbactericidalmechanismofhistidinerichbhairpinpeptideagainstgramnegativebacteria |
| publishDateSort |
2019 |
| publisher |
MDPI AG |
| recordtype |
ai |
| record_format |
ai |
| series |
International Journal of Molecular Sciences |
| source_id |
49 |
| title |
Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria |
| title_unstemmed |
Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria |
| title_full |
Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria |
| title_fullStr |
Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria |
| title_full_unstemmed |
Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria |
| title_short |
Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria |
| title_sort |
bioactivity and bactericidal mechanism of histidine-rich β-hairpin peptide against gram-negative bacteria |
| topic |
Inorganic Chemistry Organic Chemistry Physical and Theoretical Chemistry Computer Science Applications Spectroscopy Molecular Biology General Medicine Catalysis |
| url |
http://dx.doi.org/10.3390/ijms20163954 |
| publishDate |
2019 |
| physical |
3954 |
| description |
<jats:p>Antibacterial peptides (APMs) are a new type of antibacterial substance. The relationship between their structure and function remains indistinct; in particular, there is a lack of a definitive and fixed template for designing new antimicrobial peptides. Previous studies have shown that porcine Protegrin-1 (PG-1) exhibits considerable antimicrobial activity and cytotoxicity. In this study, to reduce cytotoxicity and increase cell selectivity, we designed histidine-rich peptides based on the sequence template RR(XY)2XDPGX(YX)2RR-NH2, where X represents I, W, V, and F. The results showed that the peptides form more β-hairpin structures in a lipid-rich environment that mimics cell membranes. Among them, the antimicrobial peptide HV2 showed strong antibacterial activity against Gram-negative strains and almost no toxicity to normal cells. The results of our analysis of its antibacterial mechanism showed that peptide HV2 acts on the bacterial cell membrane to increase its permeability, resulting in cell membrane disruption and death. Furthermore, peptide HV2 inhibited bacterial movement in a concentration-dependent manner and had a more robust anti-inflammatory effect by inhibiting the production of TNF-α. In summary, peptide HV2 exhibits high bactericidal activity and cell selectivity, making it a promising candidate for future use as an antibiotic.</jats:p> |
| container_issue |
16 |
| container_start_page |
0 |
| container_title |
International Journal of Molecular Sciences |
| container_volume |
20 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792343974568001542 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T16:59:52.826Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Bioactivity+and+Bactericidal+Mechanism+of+Histidine-Rich+%CE%B2-Hairpin+Peptide+Against+Gram-Negative+Bacteria&rft.date=2019-08-14&genre=article&issn=1422-0067&volume=20&issue=16&pages=3954&jtitle=International+Journal+of+Molecular+Sciences&atitle=Bioactivity+and+Bactericidal+Mechanism+of+Histidine-Rich+%CE%B2-Hairpin+Peptide+Against+Gram-Negative+Bacteria&aulast=Shan&aufirst=Anshan&rft_id=info%3Adoi%2F10.3390%2Fijms20163954&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792343974568001542 |
| author | Dong, Na, Wang, Chensi, Zhang, Tingting, Zhang, Lei, Xue, Chenyu, Feng, Xinjun, Bi, Chongpeng, Shan, Anshan |
| author_facet | Dong, Na, Wang, Chensi, Zhang, Tingting, Zhang, Lei, Xue, Chenyu, Feng, Xinjun, Bi, Chongpeng, Shan, Anshan, Dong, Na, Wang, Chensi, Zhang, Tingting, Zhang, Lei, Xue, Chenyu, Feng, Xinjun, Bi, Chongpeng, Shan, Anshan |
| author_sort | dong, na |
| container_issue | 16 |
| container_start_page | 0 |
| container_title | International Journal of Molecular Sciences |
| container_volume | 20 |
| description | <jats:p>Antibacterial peptides (APMs) are a new type of antibacterial substance. The relationship between their structure and function remains indistinct; in particular, there is a lack of a definitive and fixed template for designing new antimicrobial peptides. Previous studies have shown that porcine Protegrin-1 (PG-1) exhibits considerable antimicrobial activity and cytotoxicity. In this study, to reduce cytotoxicity and increase cell selectivity, we designed histidine-rich peptides based on the sequence template RR(XY)2XDPGX(YX)2RR-NH2, where X represents I, W, V, and F. The results showed that the peptides form more β-hairpin structures in a lipid-rich environment that mimics cell membranes. Among them, the antimicrobial peptide HV2 showed strong antibacterial activity against Gram-negative strains and almost no toxicity to normal cells. The results of our analysis of its antibacterial mechanism showed that peptide HV2 acts on the bacterial cell membrane to increase its permeability, resulting in cell membrane disruption and death. Furthermore, peptide HV2 inhibited bacterial movement in a concentration-dependent manner and had a more robust anti-inflammatory effect by inhibiting the production of TNF-α. In summary, peptide HV2 exhibits high bactericidal activity and cell selectivity, making it a promising candidate for future use as an antibiotic.</jats:p> |
| doi_str_mv | 10.3390/ijms20163954 |
| facet_avail | Online, Free |
| finc_class_facet | Physik, Informatik, Biologie, Chemie und Pharmazie |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMzM5MC9pam1zMjAxNjM5NTQ |
| imprint | MDPI AG, 2019 |
| imprint_str_mv | MDPI AG, 2019 |
| institution | DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14 |
| issn | 1422-0067 |
| issn_str_mv | 1422-0067 |
| language | English |
| last_indexed | 2024-03-01T16:59:52.826Z |
| match_str | dong2019bioactivityandbactericidalmechanismofhistidinerichbhairpinpeptideagainstgramnegativebacteria |
| mega_collection | MDPI AG (CrossRef) |
| physical | 3954 |
| publishDate | 2019 |
| publishDateSort | 2019 |
| publisher | MDPI AG |
| record_format | ai |
| recordtype | ai |
| series | International Journal of Molecular Sciences |
| source_id | 49 |
| spelling | Dong, Na Wang, Chensi Zhang, Tingting Zhang, Lei Xue, Chenyu Feng, Xinjun Bi, Chongpeng Shan, Anshan 1422-0067 MDPI AG Inorganic Chemistry Organic Chemistry Physical and Theoretical Chemistry Computer Science Applications Spectroscopy Molecular Biology General Medicine Catalysis http://dx.doi.org/10.3390/ijms20163954 <jats:p>Antibacterial peptides (APMs) are a new type of antibacterial substance. The relationship between their structure and function remains indistinct; in particular, there is a lack of a definitive and fixed template for designing new antimicrobial peptides. Previous studies have shown that porcine Protegrin-1 (PG-1) exhibits considerable antimicrobial activity and cytotoxicity. In this study, to reduce cytotoxicity and increase cell selectivity, we designed histidine-rich peptides based on the sequence template RR(XY)2XDPGX(YX)2RR-NH2, where X represents I, W, V, and F. The results showed that the peptides form more β-hairpin structures in a lipid-rich environment that mimics cell membranes. Among them, the antimicrobial peptide HV2 showed strong antibacterial activity against Gram-negative strains and almost no toxicity to normal cells. The results of our analysis of its antibacterial mechanism showed that peptide HV2 acts on the bacterial cell membrane to increase its permeability, resulting in cell membrane disruption and death. Furthermore, peptide HV2 inhibited bacterial movement in a concentration-dependent manner and had a more robust anti-inflammatory effect by inhibiting the production of TNF-α. In summary, peptide HV2 exhibits high bactericidal activity and cell selectivity, making it a promising candidate for future use as an antibiotic.</jats:p> Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria International Journal of Molecular Sciences |
| spellingShingle | Dong, Na, Wang, Chensi, Zhang, Tingting, Zhang, Lei, Xue, Chenyu, Feng, Xinjun, Bi, Chongpeng, Shan, Anshan, International Journal of Molecular Sciences, Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria, Inorganic Chemistry, Organic Chemistry, Physical and Theoretical Chemistry, Computer Science Applications, Spectroscopy, Molecular Biology, General Medicine, Catalysis |
| title | Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria |
| title_full | Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria |
| title_fullStr | Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria |
| title_full_unstemmed | Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria |
| title_short | Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria |
| title_sort | bioactivity and bactericidal mechanism of histidine-rich β-hairpin peptide against gram-negative bacteria |
| title_unstemmed | Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria |
| topic | Inorganic Chemistry, Organic Chemistry, Physical and Theoretical Chemistry, Computer Science Applications, Spectroscopy, Molecular Biology, General Medicine, Catalysis |
| url | http://dx.doi.org/10.3390/ijms20163954 |