Buforin III Analogs Bind to DNA and Actin and Inhibit Bacterial Growth

Nurit Beyth; Edna Blotnick-Rubin; Yael Houri-Haddad; Shaul Beyth; Andras Muhlrad

doi:doi:10.11648/j.ab.20180605.11

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Buforin III Analogs Bind to DNA and Actin and Inhibit Bacterial Growth

Nurit Beyth, Edna Blotnick-Rubin, Yael Houri-Haddad, Shaul Beyth, Andras Muhlrad

Published in Advances in Biochemistry (Volume 6, Issue 5)

Received: 25 October 2018 Accepted: 9 November 2018 Published: 14 December 2018

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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.

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.
Copyright	Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

Histone H2A-derived Antimicrobial Peptides, Buforin IIIB, Buforin IIIE, Antimicrobial Activity, Bundling F-actin, Binding to DNA

References

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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

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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

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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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@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}
}

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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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Author Information

Nurit Beyth

Department of Prosthodontics, Hebrew University-Hadassah School of Dental Medicine, Jerusalem, Israel
Edna Blotnick-Rubin

Department of Medical Neurobiology, Institute for Medical Research-Israel–Canada, Hebrew University of Jerusalem, Jerusalem, Israel
Yael Houri-Haddad

Department of Prosthodontics, Hebrew University-Hadassah School of Dental Medicine, Jerusalem, Israel
Shaul Beyth

Orthopedic Surgery Complex, Hadassah University Hospital, Jerusalem, Israel
Andras Muhlrad

Institute of Dental Sciences, Hebrew University-Hadassah School of Dental Medicine, Jerusalem, Israel

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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

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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

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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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@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}
}

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