Genome duplications within the Xenopodinae do not increase the multiplicity of antimicrobial peptides in Silurana paratropicalis and Xenopus andrei skin secretions

2011 ◽  
Vol 6 (2) ◽  
pp. 206-212 ◽  
Author(s):  
Milena Mechkarska ◽  
Ahmed Eman ◽  
Laurent Coquet ◽  
Leprince Jérôme ◽  
Thierry Jouenne ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Genome Duplications ◽  
Skin Secretions

Antimicrobial Peptides from Skin Secretions ofHypsiboas pulchellus(Anura: Hylidae)

2014 ◽  
Vol 77 (4) ◽  
pp. 831-841 ◽  
Author(s):  
Alvaro Siano ◽  
María Verónica Húmpola ◽  
Eliandre de Oliveira ◽  
Fernando Albericio ◽  
Arturo C. Simonetta ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Skin Secretions

Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae)

2011 ◽  
Vol 153 (3) ◽  
pp. 350-354 ◽  
Author(s):  
J. Michael Conlon ◽  
Milena Mechkarska ◽  
Eman Ahmed ◽  
Jérôme Leprince ◽  
Hubert Vaudry ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Purification And Properties ◽  
Skin Secretions ◽  
Clawed Frog

Structure-function relationships in bombinins H, antimicrobial peptides from Bombina skin secretions☆

Peptides ◽  
2000 ◽  
Vol 21 (11) ◽  
pp. 1673-1679 ◽  
Author(s):  
M.Luisa Mangoni ◽  
Nicoletta Grovale ◽  
Alessandra Giorgi ◽  
Giuseppina Mignogna ◽  
Maurizio Simmaco ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Structure Function ◽  
Skin Secretions

scholarly journals Development of Antimicrobial Peptides from Amphibians

Antibiotics ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 772
Author(s):  
Maria Luisa Mangoni ◽  
Bruno Casciaro
Keyword(s):  
Xenopus Laevis ◽  
Antimicrobial Peptides ◽  
Anuran Species ◽  
Skin Secretions

Since the discovery of magainins from the skin secretions of the African toad Xenopus laevis by Michael Zasloff in 1987, an increasing number of antimicrobial peptides (AMPs) has been identified in different anuran species and studied in detail [...]

scholarly journals Development and Challenges of Antimicrobial Peptides for Therapeutic Applications

Antibiotics ◽  
2020 ◽  
Vol 9 (1) ◽  
pp. 24 ◽  
Author(s):  
Charles H. Chen ◽  
Timothy K. Lu
Keyword(s):  
Antimicrobial Peptides ◽  
Soil Bacteria ◽  
Bacterial Infections ◽  
Mechanisms Of Action ◽  
The Body ◽  
Antimicrobial Drugs ◽  
Skin Secretions ◽  
Approved Drugs ◽  
Topical Medications ◽  
Fda Approved Drugs

More than 3000 antimicrobial peptides (AMPs) have been discovered, seven of which have been approved by the U.S. Food and Drug Administration (FDA). Now commercialized, these seven peptides have mostly been utilized for topical medications, though some have been injected into the body to treat severe bacterial infections. To understand the translational potential for AMPs, we analyzed FDA-approved drugs in the FDA drug database. We examined their physicochemical properties, secondary structures, and mechanisms of action, and compared them with the peptides in the AMP database. All FDA-approved AMPs were discovered in Gram-positive soil bacteria, and 98% of known AMPs also come from natural sources (skin secretions of frogs and toxins from different species). However, AMPs can have undesirable properties as drugs, including instability and toxicity. Thus, the design and construction of effective AMPs require an understanding of the mechanisms of known peptides and their effects on the human body. This review provides an overview to guide the development of AMPs that can potentially be used as antimicrobial drugs.

Novel antimicrobial peptides isolated from the skin secretions of Hainan odorous frog, Odorrana hainanensis

Peptides ◽  
2012 ◽  
Vol 35 (2) ◽  
pp. 285-290 ◽  
Author(s):  
Hui Wang ◽  
Zhijun Yu ◽  
Yuhong Hu ◽  
Fengjiao Li ◽  
Limeng Liu ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Skin Secretions

scholarly journals Skin secretions of Rana saharica frogs reveal antimicrobial peptides esculentins-1 and -1B and brevinins-1E and -2EC with novel insulin releasing activity

2006 ◽  
Vol 188 (1) ◽  
pp. 1-9 ◽  
Author(s):  
L Marenah ◽  
P R Flatt ◽  
D F Orr ◽  
C Shaw ◽  
Y H A Abdel-Wahab
Keyword(s):  
Antimicrobial Peptides ◽  
Insulin Release ◽  
Skin Surface ◽  
Bioactive Molecules ◽  
Peptide Family ◽  
Insulin Secretagogues ◽  
Frog Species ◽  
Molecular Masses ◽  
Skin Secretions ◽  
Toxic Peptides

Skin secretions of Rana saharica were evaluated for the isolation and characterisation of novel insulinotropic peptides. Crude secretions obtained from young adult frogs by mild electrical stimulation of the dorsal skin surface were purified by reverse phase HPLC yielding 80 fractions. In acute 20-min incubations with glucose responsive BRIN-BD11 cells, fractions 36–43, 46–54 and 57–63 significantly stimulated insulin release by 2- to 8-fold compared with 5.6 mM glucose alone. Pooled fractions in the latter two bands were rechromatographed to reveal 9 homogenous peaks, which elicited significant 1.3- to 3.5-fold increases in insulin release (P < 0.05). Structural analysis of the most potent non-toxic peptides was performed by mass spectrometry and automated Edman degradation. This revealed four major insulin-releasing peaks with molecular masses of 2676.9 Da, 3519.3 Da, 4920.4 Da and 4801.2 Da respectively. These peptides were found to be identical to brevinin-1E, brevinin-2EC, esculentin-1 and esculentin-1B, which belong to the group of antimicrobial peptides isolated from skin secretions of various Rana frog species. Preliminary studies on the mechanism underlying the insulinotropic actions of esculentins-1 and -1B suggested possible involvement of both cyclic AMP–protein kinase A and –C-dependent G-protein sensitive pathways. These data indicate that the skin secretions of Rana saharica frogs contain bioactive molecules with significant insulin-releasing activity. Relatives of the brevinin/esculentin peptide family merit further investigation as novel insulin secretagogues.

Sign in / Sign up

Export Citation Format

Share Document