Difference between revisions of "Part:BBa K4147009"
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<partinfo>BBa_K4147009 short</partinfo> | <partinfo>BBa_K4147009 short</partinfo> | ||
| − | Antimicrobial protein from the arboreal tree frog <i>Phyllomedusa bicolor</i>, dermaseptin-b1 gene (AKA MsrA2) fused with a 6X Hist tag for purification by metal affinity chromatography. | + | Antimicrobial protein from the arboreal tree frog <i>Phyllomedusa bicolor</i>, dermaseptin-b1 gene (AKA MsrA2) (BBa_K2577001) fused with a 6X-Hist tag for purification by metal affinity chromatography. |
| − | |||
===Usage and Biology=== | ===Usage and Biology=== | ||
| + | <p align="justify"> | ||
| + | Dermaseptins (DRSs) are peptides produced by Hylid frogs, a group of ɑ-helical shaped polycationic and short peptides (21-34 residues) containing a highly preserved tryptophan residue on N-terminal 3rd position, with hydrophobic residues and the polar cationic residues clusters in opposite sides [1]. | ||
| + | The majority of the dermaseptin family peptides exhibit a wide variety of antibacterial activities. A broad range of microorganisms, including mollicutes, bacteria, fungi, protozoa, yeast, and enveloped viruses are all susceptible to the dermaseptins. Despite having a very similar sequence, the dermaseptins vary in how well they can neutralize different substances [2]. | ||
| + | Dermaseptins also exhibit efficacy against various kinds of human cancer, making them anticancer peptides in addition to their antimicrobial capabilities.[1]. </p> | ||
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<partinfo>BBa_K4147009 parameters</partinfo> | <partinfo>BBa_K4147009 parameters</partinfo> | ||
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| + | ===REFERENCES=== | ||
| + | [1] Bartels J. et al. Dermaseptins, Multifunctional Antimicrobial Peptides: A Review of Their Pharmacology, Effectivity, Mechanism of Action, and Possible Future Directions. | ||
| + | |||
| + | [2] Nicolas, P., & el Amri, C. (2009). The dermaseptin superfamily: A gene-based combinatorial library of antimicrobial peptides. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1788(8), 1537–1550. | ||
Revision as of 05:56, 10 October 2022
MsrA2 antimicrobial protein for purification with 6X-His tag
Antimicrobial protein from the arboreal tree frog Phyllomedusa bicolor, dermaseptin-b1 gene (AKA MsrA2) (BBa_K2577001) fused with a 6X-Hist tag for purification by metal affinity chromatography.
Usage and Biology
Dermaseptins (DRSs) are peptides produced by Hylid frogs, a group of ɑ-helical shaped polycationic and short peptides (21-34 residues) containing a highly preserved tryptophan residue on N-terminal 3rd position, with hydrophobic residues and the polar cationic residues clusters in opposite sides [1]. The majority of the dermaseptin family peptides exhibit a wide variety of antibacterial activities. A broad range of microorganisms, including mollicutes, bacteria, fungi, protozoa, yeast, and enveloped viruses are all susceptible to the dermaseptins. Despite having a very similar sequence, the dermaseptins vary in how well they can neutralize different substances [2]. Dermaseptins also exhibit efficacy against various kinds of human cancer, making them anticancer peptides in addition to their antimicrobial capabilities.[1].
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
REFERENCES
[1] Bartels J. et al. Dermaseptins, Multifunctional Antimicrobial Peptides: A Review of Their Pharmacology, Effectivity, Mechanism of Action, and Possible Future Directions.
[2] Nicolas, P., & el Amri, C. (2009). The dermaseptin superfamily: A gene-based combinatorial library of antimicrobial peptides. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1788(8), 1537–1550.