Antimicrobial activities and action mechanism studies of transportan 10 and its analogues against multidrug-resistant bacteria

2015 ◽  
Vol 21 (7) ◽  
pp. 599-607 ◽  
Author(s):  
Junqiu Xie ◽  
Yuanmei Gou ◽  
Qian Zhao ◽  
Sisi Li ◽  
Wei Zhang ◽  
...  
Keyword(s):  
Multidrug Resistant ◽  
Antimicrobial Activities ◽  
Resistant Bacteria ◽  
Action Mechanism ◽  
Multidrug Resistant Bacteria

Action mechanism of melittin-derived antimicrobial peptides, MDP1 and MDP2, de novo designed against multidrug resistant bacteria

Amino Acids ◽  
2018 ◽  
Vol 50 (9) ◽  
pp. 1231-1243 ◽  
Author(s):  
Reza Akbari ◽  
Mojdeh Hakemi Vala ◽  
Ali Hashemi ◽  
Hossein Aghazadeh ◽  
Jean-Marc Sabatier ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
De Novo ◽  
Multidrug Resistant ◽  
Resistant Bacteria ◽  
Action Mechanism ◽  
Multidrug Resistant Bacteria

scholarly journals Potent Antimicrobial and Antibiofilm Activities of Feleucin-K3 Analogs Modified by α-(4-Pentenyl)-Ala against Multidrug-Resistant Bacteria

Biomolecules ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 761
Author(s):  
Xiaomin Guo ◽  
Tiantian Yan ◽  
Jing Rao ◽  
Xin Yue ◽  
Xiong Pei ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Biofilm Formation ◽  
Methicillin Resistant Staphylococcus Aureus ◽  
Cytoplasmic Membrane ◽  
Multidrug Resistant ◽  
Antimicrobial Activities ◽  
Unnatural Amino Acid ◽  
Cellular Component ◽  
Resistant Bacteria ◽  
Multidrug Resistant Bacteria

The dramatic increase in antimicrobial resistance (AMR) highlights an urgent need to develop new antimicrobial therapies. Thus, antimicrobial peptides (AMPs) have emerged as promising novel antibiotic alternatives. Feleucin-K3 is an amphiphilic α-helical nonapeptide that has powerful antimicrobial activity. In our previous study, it was found that the fourth residue of Feleucin-K3 is important for antimicrobial activity. After α-(4-pentenyl)-Ala was introduced into this position, both the antimicrobial activity and stability were greatly improved. Herein, to improve the limitations of Feleucin-K3, this unnatural amino acid was further introduced into different positions of Feleucin-K3. Among these synthetic Feleucin-K3 analogs, the N-terminal-substituted analog Feleucin-K65 (K65) and C-terminal-substituted analog Feleucin-K70 (K70) had preferable antimicrobial activity. In particular, their antimicrobial activities against multidrug-resistant bacteria were more potent than that of antibiotics. The stabilities of these peptides in salt and serum environments were improved compared with those of Feleucin-K3. In addition, these analogs had low hemolytic activity and AMR. More importantly, they effectively inhibited biofilm formation and exhibited considerable efficacy compared with traditional antibiotics against biofilm infection caused by methicillin-resistant Staphylococcus aureus (MRSA). In antimicrobial mechanism studies, K65 and K70 mainly permeated the outer membrane and depolarized the cytoplasmic membrane, resulting in cellular component leakage and cell death. In summary, analogs K65 and K70 are potential antimicrobial alternatives to solve the antibiotic crisis.

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