Inhibitory and antimicrobial activities of OGTI and HV-BBI peptides, fragments and analogs derived from amphibian skin

Peptides ◽  
2012 ◽  
Vol 35 (2) ◽  
pp. 276-284 ◽  
Author(s):  
Dawid Dębowski ◽  
Rafał Łukajtis ◽  
Anna Łęgowska ◽  
Natalia Karna ◽  
Michał Pikuła ◽  
...  
2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Lilin Ge ◽  
Peng Lyu ◽  
Mei Zhou ◽  
Huiling Zhang ◽  
Yuantai Wan ◽  
...  

Tryptophyllins are a diverse family of amphibian peptides originally found in extracts of phyllomedusine frog skin by chemical means. Their biological activities remain obscure. Here we describe the isolation and preliminary pharmacological characterization of a novel type 2 tryptophyllin, named AcT-2, from the skin secretion of the red-eyed leaf frog,Agalychnis callidryas. The peptide was initially identified during smooth muscle pharmacological screening of skin secretion HPLC fractions and the unique primary structure—GMRPPWF-NH2—was established by both Edman degradation and electrospray MS/MS fragmentation sequencing. A. cDNA encoding the biosynthetic precursor of AcT-2 was successfully cloned from a skin secretion-derived cDNA library by means of RACE PCR and this contained an open-reading frame consisting of 62 amino acid residues with a single AcT-2 encoding sequence located towards the C-terminus. A synthetic replicate of AcT-2 was found to relax arterial smooth muscle (EC50= 5.1 nM) and to contract rat urinary bladder smooth muscle (EC50= 9.3 μM). The peptide could also inhibit the growth of the microorganisms,Staphylococcus aureus, (MIC = 256 mg/L)Escherichia coli(MIC = 512 mg/L), andCandida albicans(128 mg/L). AcT-2 is thus the first amphibian skin tryptophyllin found to possess both myotropic and antimicrobial activities.


2018 ◽  
Vol 19 (8) ◽  
pp. 2170 ◽  
Author(s):  
Carolina Muñoz-Camargo ◽  
Vivian Salazar ◽  
Laura Barrero-Guevara ◽  
Sandra Camargo ◽  
Angela Mosquera ◽  
...  

Amphibian skin is a rich source of natural compounds with diverse antimicrobial and immune defense properties. Our previous studies showed that the frog skin secretions obtained by skin micro-organs from various species of Colombian anurans have antimicrobial activities against bacteria and viruses. We purified for the first time two antimicrobial peptides from the skin micro-organs of the Orinoco lime treefrog (Sphaenorhynchus lacteus) that correspond to Buforin II (BF2) and Frenatin 2.3S (F2.3S). Here, we have synthesized the two peptides and tested them against Gram-negative and Gram-positive bacteria, observing an effective bactericidal activity at micromolar concentrations. Evaluation of BF2 and F2.3S membrane destabilization activity on bacterial cell cultures and synthetic lipid bilayers reveals a distinct membrane interaction mechanism. BF2 agglutinates E. coli cells and synthetic vesicles, whereas F2.3S shows a high depolarization and membrane destabilization activities. Interestingly, we found that F2.3S is able to internalize within bacterial cells and can bind nucleic acids, as previously reported for BF2. Moreover, bacterial exposure to both peptides alters the expression profile of genes related to stress and resistance response. Overall, these results show the multifaceted mechanism of action of both antimicrobial peptides that can provide alternative tools in the fight against bacterial resistance.


Planta Medica ◽  
2010 ◽  
Vol 76 (12) ◽  
Author(s):  
M Sharifzadeh ◽  
F Yousefbeyk ◽  
G Amin ◽  
M Salehi Sormaghi ◽  
B Azadi ◽  
...  

Planta Medica ◽  
2010 ◽  
Vol 76 (12) ◽  
Author(s):  
P Thongmuang ◽  
Y Sudjaroen ◽  
R Owen

2019 ◽  
Author(s):  
A Filip ◽  
I Boz ◽  
S Dunca ◽  
G-A Ștefan ◽  
M-M Zamfirache

Planta Medica ◽  
2007 ◽  
Vol 73 (09) ◽  
Author(s):  
S Stojièević ◽  
I Stanisavljević ◽  
D Velièković ◽  
V Veljković ◽  
M Lazić

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