Buforin is a cationic antimicrobial peptide (AMP) from the stomach of toads. Buforin II is a derivative of this naturally occurring peptide. Buforin IIB is a synthetic analog of buforin II containing a model α-helical sequence (3xRLLR) at the C-terminus. To further increase the antimicrobial activity and decrease toxicity to eukaryotic cells, new derivatives (buforin III analogs) were designed by substituting amino acids in the buforin IIB sequence. In this work, the antimicrobial activity and the actin- and DNA-binding characteristics of buforin IIIB (RVVRQWPIGRVVRRVVRRVVR) and the newly synthetized buforin IIIE (RLLLRQWPIGRLLRRLLRRLLR) were studied. The antimicrobial activity of buforin IIIB (measured against E. coli and E. faecalis) was significantly greater than that of buforin IIIE, while both peptides were nontoxic to macrophages at the minimal concentrations required to inhibit microbial growth. Actin, which inhibited the antimicrobial activity of the two buforin III analogs, was bundled by both peptides; however, less buforin IIIE than buforin IIIB was needed for bundling. Higher levels of NaCl were needed to unbundle actin bundled by buforin IIIE than actin bundled by buforin IIIB, which indicates that buforin IIIE binds more strongly to actin than buforin IIIB. Actin bundled by either peptide was dissociated with the same concentration of DNA; however, buforin IIIE bound more strongly to DNA than buforin IIIB. These results contribute to the understanding of the antimicrobial mechanism of cationic AMPs in general and histone-derived peptides in particular.
| Published in | Advances in Biochemistry (Volume 6, Issue 5) |
| DOI | 10.11648/j.ab.20180605.11 |
| Page(s) | 39-46 |
| Creative Commons |
This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
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Copyright © The Author(s), 2018. Published by Science Publishing Group |
Histone H2A-derived Antimicrobial Peptides, Buforin IIIB, Buforin IIIE, Antimicrobial Activity, Bundling F-actin, Binding to DNA
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APA Style
Nurit Beyth, Edna Blotnick-Rubin, Yael Houri-Haddad, Shaul Beyth, Andras Muhlrad. (2018). Buforin III Analogs Bind to DNA and Actin and Inhibit Bacterial Growth. Advances in Biochemistry, 6(5), 39-46. https://doi.org/10.11648/j.ab.20180605.11
ACS Style
Nurit Beyth; Edna Blotnick-Rubin; Yael Houri-Haddad; Shaul Beyth; Andras Muhlrad. Buforin III Analogs Bind to DNA and Actin and Inhibit Bacterial Growth. Adv. Biochem. 2018, 6(5), 39-46. doi: 10.11648/j.ab.20180605.11
AMA Style
Nurit Beyth, Edna Blotnick-Rubin, Yael Houri-Haddad, Shaul Beyth, Andras Muhlrad. Buforin III Analogs Bind to DNA and Actin and Inhibit Bacterial Growth. Adv Biochem. 2018;6(5):39-46. doi: 10.11648/j.ab.20180605.11
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Download@article{10.11648/j.ab.20180605.11,
author = {Nurit Beyth and Edna Blotnick-Rubin and Yael Houri-Haddad and Shaul Beyth and Andras Muhlrad},
title = {Buforin III Analogs Bind to DNA and Actin and Inhibit Bacterial Growth},
journal = {Advances in Biochemistry},
volume = {6},
number = {5},
pages = {39-46},
doi = {10.11648/j.ab.20180605.11},
url = {https://doi.org/10.11648/j.ab.20180605.11},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ab.20180605.11},
abstract = {Buforin is a cationic antimicrobial peptide (AMP) from the stomach of toads. Buforin II is a derivative of this naturally occurring peptide. Buforin IIB is a synthetic analog of buforin II containing a model α-helical sequence (3xRLLR) at the C-terminus. To further increase the antimicrobial activity and decrease toxicity to eukaryotic cells, new derivatives (buforin III analogs) were designed by substituting amino acids in the buforin IIB sequence. In this work, the antimicrobial activity and the actin- and DNA-binding characteristics of buforin IIIB (RVVRQWPIGRVVRRVVRRVVR) and the newly synthetized buforin IIIE (RLLLRQWPIGRLLRRLLRRLLR) were studied. The antimicrobial activity of buforin IIIB (measured against E. coli and E. faecalis) was significantly greater than that of buforin IIIE, while both peptides were nontoxic to macrophages at the minimal concentrations required to inhibit microbial growth. Actin, which inhibited the antimicrobial activity of the two buforin III analogs, was bundled by both peptides; however, less buforin IIIE than buforin IIIB was needed for bundling. Higher levels of NaCl were needed to unbundle actin bundled by buforin IIIE than actin bundled by buforin IIIB, which indicates that buforin IIIE binds more strongly to actin than buforin IIIB. Actin bundled by either peptide was dissociated with the same concentration of DNA; however, buforin IIIE bound more strongly to DNA than buforin IIIB. These results contribute to the understanding of the antimicrobial mechanism of cationic AMPs in general and histone-derived peptides in particular.},
year = {2018}
}
TY - JOUR T1 - Buforin III Analogs Bind to DNA and Actin and Inhibit Bacterial Growth AU - Nurit Beyth AU - Edna Blotnick-Rubin AU - Yael Houri-Haddad AU - Shaul Beyth AU - Andras Muhlrad Y1 - 2018/12/14 PY - 2018 N1 - https://doi.org/10.11648/j.ab.20180605.11 DO - 10.11648/j.ab.20180605.11 T2 - Advances in Biochemistry JF - Advances in Biochemistry JO - Advances in Biochemistry SP - 39 EP - 46 PB - Science Publishing Group SN - 2329-0862 UR - https://doi.org/10.11648/j.ab.20180605.11 AB - Buforin is a cationic antimicrobial peptide (AMP) from the stomach of toads. Buforin II is a derivative of this naturally occurring peptide. Buforin IIB is a synthetic analog of buforin II containing a model α-helical sequence (3xRLLR) at the C-terminus. To further increase the antimicrobial activity and decrease toxicity to eukaryotic cells, new derivatives (buforin III analogs) were designed by substituting amino acids in the buforin IIB sequence. In this work, the antimicrobial activity and the actin- and DNA-binding characteristics of buforin IIIB (RVVRQWPIGRVVRRVVRRVVR) and the newly synthetized buforin IIIE (RLLLRQWPIGRLLRRLLRRLLR) were studied. The antimicrobial activity of buforin IIIB (measured against E. coli and E. faecalis) was significantly greater than that of buforin IIIE, while both peptides were nontoxic to macrophages at the minimal concentrations required to inhibit microbial growth. Actin, which inhibited the antimicrobial activity of the two buforin III analogs, was bundled by both peptides; however, less buforin IIIE than buforin IIIB was needed for bundling. Higher levels of NaCl were needed to unbundle actin bundled by buforin IIIE than actin bundled by buforin IIIB, which indicates that buforin IIIE binds more strongly to actin than buforin IIIB. Actin bundled by either peptide was dissociated with the same concentration of DNA; however, buforin IIIE bound more strongly to DNA than buforin IIIB. These results contribute to the understanding of the antimicrobial mechanism of cationic AMPs in general and histone-derived peptides in particular. VL - 6 IS - 5 ER -
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