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Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18
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| Zeitschriftentitel: | Molecules |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | Molecules, 25, 2020, 3, S. 485 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
MDPI AG
|
| Schlagwörter: |
| author_facet |
Teng, Tieshan Li, Xianghui Zhang, Lei Li, Yanzhang Teng, Tieshan Li, Xianghui Zhang, Lei Li, Yanzhang |
|---|---|
| author |
Teng, Tieshan Li, Xianghui Zhang, Lei Li, Yanzhang |
| spellingShingle |
Teng, Tieshan Li, Xianghui Zhang, Lei Li, Yanzhang Molecules Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18 Chemistry (miscellaneous) Analytical Chemistry Organic Chemistry Physical and Theoretical Chemistry Molecular Medicine Drug Discovery Pharmaceutical Science |
| author_sort |
teng, tieshan |
| spelling |
Teng, Tieshan Li, Xianghui Zhang, Lei Li, Yanzhang 1420-3049 MDPI AG Chemistry (miscellaneous) Analytical Chemistry Organic Chemistry Physical and Theoretical Chemistry Molecular Medicine Drug Discovery Pharmaceutical Science http://dx.doi.org/10.3390/molecules25030485 <jats:p>Pantoea dispersa W18, isolated from contaminated soil, was found to exert antimicrobial activity against Mycobacterium species, including Mycobacterium tuberculosis, an important human pathogen. Here, the anti-mycobacterial compound produced by Pantoea dispersa W18 was purified by a combination of hydrophobic interaction chromatography, cation exchange chromatography, and reverse phase HPLC. Active compounds from Pantoea dispersa W18 were identified as a natural peptide named pantocin wh-1 with a 1927 Da molecular weight. The primary structure of this compound was detected by N-terminal amino acid sequencing. The amino acid sequence of pantocin wh-1 consisted of 16 amino acid residues with a cyclic structure. The pantocin wh-1 could be inactivated by protease K, but was heat stable and unaffected by pH (2–12). However, the activity was not completely inactivated by trypsin and pepsin. This is the first report of a cyclic polypeptide purified from a strain of Pantoea dispersa.</jats:p> Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18 Molecules |
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| title |
Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18 |
| title_unstemmed |
Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18 |
| title_full |
Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18 |
| title_fullStr |
Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18 |
| title_full_unstemmed |
Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18 |
| title_short |
Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18 |
| title_sort |
identification and characterization of pantocin wh-1, a novel cyclic polypeptide produced by pantoea dispersa w18 |
| topic |
Chemistry (miscellaneous) Analytical Chemistry Organic Chemistry Physical and Theoretical Chemistry Molecular Medicine Drug Discovery Pharmaceutical Science |
| url |
http://dx.doi.org/10.3390/molecules25030485 |
| publishDate |
2020 |
| physical |
485 |
| description |
<jats:p>Pantoea dispersa W18, isolated from contaminated soil, was found to exert antimicrobial activity against Mycobacterium species, including Mycobacterium tuberculosis, an important human pathogen. Here, the anti-mycobacterial compound produced by Pantoea dispersa W18 was purified by a combination of hydrophobic interaction chromatography, cation exchange chromatography, and reverse phase HPLC. Active compounds from Pantoea dispersa W18 were identified as a natural peptide named pantocin wh-1 with a 1927 Da molecular weight. The primary structure of this compound was detected by N-terminal amino acid sequencing. The amino acid sequence of pantocin wh-1 consisted of 16 amino acid residues with a cyclic structure. The pantocin wh-1 could be inactivated by protease K, but was heat stable and unaffected by pH (2–12). However, the activity was not completely inactivated by trypsin and pepsin. This is the first report of a cyclic polypeptide purified from a strain of Pantoea dispersa.</jats:p> |
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| author | Teng, Tieshan, Li, Xianghui, Zhang, Lei, Li, Yanzhang |
| author_facet | Teng, Tieshan, Li, Xianghui, Zhang, Lei, Li, Yanzhang, Teng, Tieshan, Li, Xianghui, Zhang, Lei, Li, Yanzhang |
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| description | <jats:p>Pantoea dispersa W18, isolated from contaminated soil, was found to exert antimicrobial activity against Mycobacterium species, including Mycobacterium tuberculosis, an important human pathogen. Here, the anti-mycobacterial compound produced by Pantoea dispersa W18 was purified by a combination of hydrophobic interaction chromatography, cation exchange chromatography, and reverse phase HPLC. Active compounds from Pantoea dispersa W18 were identified as a natural peptide named pantocin wh-1 with a 1927 Da molecular weight. The primary structure of this compound was detected by N-terminal amino acid sequencing. The amino acid sequence of pantocin wh-1 consisted of 16 amino acid residues with a cyclic structure. The pantocin wh-1 could be inactivated by protease K, but was heat stable and unaffected by pH (2–12). However, the activity was not completely inactivated by trypsin and pepsin. This is the first report of a cyclic polypeptide purified from a strain of Pantoea dispersa.</jats:p> |
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| spelling | Teng, Tieshan Li, Xianghui Zhang, Lei Li, Yanzhang 1420-3049 MDPI AG Chemistry (miscellaneous) Analytical Chemistry Organic Chemistry Physical and Theoretical Chemistry Molecular Medicine Drug Discovery Pharmaceutical Science http://dx.doi.org/10.3390/molecules25030485 <jats:p>Pantoea dispersa W18, isolated from contaminated soil, was found to exert antimicrobial activity against Mycobacterium species, including Mycobacterium tuberculosis, an important human pathogen. Here, the anti-mycobacterial compound produced by Pantoea dispersa W18 was purified by a combination of hydrophobic interaction chromatography, cation exchange chromatography, and reverse phase HPLC. Active compounds from Pantoea dispersa W18 were identified as a natural peptide named pantocin wh-1 with a 1927 Da molecular weight. The primary structure of this compound was detected by N-terminal amino acid sequencing. The amino acid sequence of pantocin wh-1 consisted of 16 amino acid residues with a cyclic structure. The pantocin wh-1 could be inactivated by protease K, but was heat stable and unaffected by pH (2–12). However, the activity was not completely inactivated by trypsin and pepsin. This is the first report of a cyclic polypeptide purified from a strain of Pantoea dispersa.</jats:p> Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18 Molecules |
| spellingShingle | Teng, Tieshan, Li, Xianghui, Zhang, Lei, Li, Yanzhang, Molecules, Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18, Chemistry (miscellaneous), Analytical Chemistry, Organic Chemistry, Physical and Theoretical Chemistry, Molecular Medicine, Drug Discovery, Pharmaceutical Science |
| title | Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18 |
| title_full | Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18 |
| title_fullStr | Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18 |
| title_full_unstemmed | Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18 |
| title_short | Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18 |
| title_sort | identification and characterization of pantocin wh-1, a novel cyclic polypeptide produced by pantoea dispersa w18 |
| title_unstemmed | Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18 |
| topic | Chemistry (miscellaneous), Analytical Chemistry, Organic Chemistry, Physical and Theoretical Chemistry, Molecular Medicine, Drug Discovery, Pharmaceutical Science |
| url | http://dx.doi.org/10.3390/molecules25030485 |