Mechanism of Action of the Antimicrobial Peptide Buforin II: Buforin II Kills Microorganisms by Penetrating the Cell Membrane and Inhibiting Cellular Functions

1998 ◽  
Vol 244 (1) ◽  
pp. 253-257 ◽  
Author(s):  
Chan Bae Park ◽  
Hun Sik Kim ◽  
Sun Chang Kim
Keyword(s):  
Cell Membrane ◽  
Antimicrobial Peptide ◽  
Mechanism Of Action ◽  
Cellular Functions

scholarly journals Beneficial Impacts of Incorporating the Non-Natural Amino Acid Azulenyl-Alanine into the Trp-Rich Antimicrobial Peptide buCATHL4B

Biomolecules ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 421
Author(s):  
Areetha R. D’Souza ◽  
Matthew R. Necelis ◽  
Alona Kulesha ◽  
Gregory A. Caputo ◽  
Olga V. Makhlynets
Keyword(s):  
Amino Acid ◽  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Mechanism Of Action ◽  
Bactericidal Activity ◽  
Antimicrobial Agents ◽  
Human Cells ◽  
Side Chains ◽  
Natural Amino Acid ◽  
Proteolytic Stability

Antimicrobial peptides (AMPs) present a promising scaffold for the development of potent antimicrobial agents. Substitution of tryptophan by non-natural amino acid Azulenyl-Alanine (AzAla) would allow studying the mechanism of action of AMPs by using unique properties of this amino acid, such as ability to be excited separately from tryptophan in a multi-Trp AMPs and environmental insensitivity. In this work, we investigate the effect of Trp→AzAla substitution in antimicrobial peptide buCATHL4B (contains three Trp side chains). We found that antimicrobial and bactericidal activity of the original peptide was preserved, while cytocompatibility with human cells and proteolytic stability was improved. We envision that AzAla will find applications as a tool for studies of the mechanism of action of AMPs. In addition, incorporation of this non-natural amino acid into AMP sequences could enhance their application properties.

scholarly journals Antibacterial activity and mechanism of action of analogues derived from the antimicrobial peptide mBjAMP1 isolated from Branchiostoma japonicum

2018 ◽  
Vol 73 (8) ◽  
pp. 2054-2063 ◽  
Author(s):  
Jonggwan Park ◽  
Hee Kyoung Kang ◽  
Moon-Chang Choi ◽  
Jeong Don Chae ◽  
Byoung Kwan Son ◽  
...  
Keyword(s):  
Antibacterial Activity ◽  
Antimicrobial Peptide ◽  
Mechanism Of Action

scholarly journals Activity of Antimicrobial Peptide Aggregates Decreases with Increased Cell Membrane Embedding Free Energy Cost

Biochemistry ◽  
2018 ◽  
Vol 57 (18) ◽  
pp. 2606-2610 ◽  
Author(s):  
Rongfeng Zou ◽  
Xiaomin Zhu ◽  
Yaoquan Tu ◽  
Junchen Wu ◽  
Markita P. Landry
Keyword(s):  
Free Energy ◽  
Cell Membrane ◽  
Antimicrobial Peptide ◽  
Energy Cost

An antimicrobial peptide screened from casein hydrolyzate by Saccharomyces cerevisiae cell membrane affinity method

Food Control ◽  
2015 ◽  
Vol 50 ◽  
pp. 413-422 ◽  
Author(s):  
Wenting Tang ◽  
Huaning Yuan ◽  
Hui Zhang ◽  
Li Wang ◽  
Haifeng Qian ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Membrane ◽  
Antimicrobial Peptide ◽  
Membrane Affinity ◽  
Casein Hydrolyzate

scholarly journals PvD1 defensin, a plant antimicrobial peptide with inhibitory activity against Leishmania amazonensis

2015 ◽  
Vol 35 (5) ◽  
Author(s):  
Viviane V. do Nascimento ◽  
Érica de O. Mello ◽  
Laís P. Carvalho ◽  
Edésio J.T. de Melo ◽  
André de O. Carvalho ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Antimicrobial Peptide ◽  
Inhibitory Activity ◽  
Membrane Permeabilization ◽  
Leishmania Amazonensis ◽  
Cell Membrane Permeabilization ◽  
Intracellular Target

PvD1 was able to inhibit the proliferation of Leishmania amazonensis promastigotes; PvD1 caused cell membrane permeabilization and alterations in the cytoplasmic contents of these cells; PvD1 was internalized in these cells, what suggests a possible intracellular target.

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