Characterization and action mode of Gluconacin, a bacteriocin with antimicrobial activity against Xanthomonas albilineans

2021 ◽  
Author(s):  
Elizabeth Teixeira Almeida Ramos ◽  
Carlos Henrique Salvino Gadelha Meneses ◽  
Marcia Soares Vidal ◽  
José Ivo Baldani
Biomolecules ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 1254 ◽  
Author(s):  
Xi Chen ◽  
Dong Chen ◽  
Linyuan Huang ◽  
Xiaoling Chen ◽  
Mei Zhou ◽  
...  

The peptides from the ranacyclin family share similar active disulphide loop with plant-derived Bowman–Birk type inhibitors, some of which have the dual activities of trypsin inhibition and antimicrobial. Herein, a novel Bowman–Birk type trypsin inhibitor of the ranacyclin family was identified from the skin secretion of broad-folded frog (Sylvirana latouchii) by molecular cloning method and named as SL-BBI. After chemical synthesis, it was proved to be a potent inhibitor of trypsin with a Ki value of 230.5 nM and showed weak antimicrobial activity against tested microorganisms. Modified analogue K-SL maintains the original inhibitory activity with a Ki value of 77.27 nM while enhancing the antimicrobial activity. After the substitution of active P1 site to phenylalanine and P2′ site to isoleucine, F-SL regenerated its inhibitory activity on chymotrypsin with a Ki value of 309.3 nM and exhibited antiproliferative effects on PC-3, MCF-7 and a series of non-small cell lung cancer cell lines without cell membrane damage. The affinity of F-SL for the β subunits in the yeast 20S proteasome showed by molecular docking simulations enriched the understanding of the possible action mode of Bowman–Birk type inhibitors. Further mechanistic studies have shown that F-SL can activate caspase 3/7 in H157 cells and induce apoptosis, which means it has the potential to become an anticancer agent.


2013 ◽  
Vol 57 (10) ◽  
pp. 4632-4639 ◽  
Author(s):  
Kairong Wang ◽  
Wen Dang ◽  
Jiexi Yan ◽  
Ru Chen ◽  
Xin Liu ◽  
...  

ABSTRACTWith the extensive use of antibiotics, multidrug-resistant bacteria emerge frequently. New antimicrobial agents with novel modes of action are urgently needed. It is now widely accepted that antimicrobial peptides (AMPs) could be promising alternatives to conventional antibiotics. In this study, we aimed to study the antimicrobial activity and mechanism of action of protonectin, a cationic peptide from the venom of the neotropical social waspAgelaia pallipes pallipes. We demonstrated that protonectin exhibits potent antimicrobial activity against a spectrum of bacteria, including multidrug-resistant strains. To further understand this mechanism, the structural features of protonectin and its analogs were studied by circular dichroism (CD). The CD spectra demonstrated that protonectin and its natural analog polybia-CP formed a typical α-helical conformation in the membrane-mimicking environment, while its proline-substituted analog had much lower or even no α-helix conformation. Molecular dynamics simulations indicated that the α-helical conformation in the membrane is required for the exhibition of antibacterial activity. In conclusion, protonectin exhibits potent antimicrobial activity by disruption of the integrity of the bacterial membrane, and its α-helical confirmation in the membrane is essential for this action.


Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
L Araujo ◽  
N Padilla ◽  
GG Llanos ◽  
IL Bazzocchi ◽  
L Moujir

Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
R Łos ◽  
K Skalicka-Wozniak ◽  
J Widelski ◽  
A Malm ◽  
K Głowniak

Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
I Kosalec ◽  
M Zovko ◽  
K Sankovic ◽  
D Kremer ◽  
S Pepeljnjak

Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
SN Ebrahimi ◽  
M Yousefzadi ◽  
A Sonboli ◽  
F Miraghasi ◽  
S Ghiasi ◽  
...  

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