Isolation of a trefoil factor BmTFF3 from frog skin secretions that can form a functional complex with aerolysin-like pore-forming protein in host defensive system

Toxicon ◽  
2019 ◽  
Vol 158 ◽  
pp. S86
Author(s):  
Ling-Zhen Liu ◽  
Qi-Quan Wang ◽  
Wen-Hui Lee ◽  
Xiao-Long Guo ◽  
Yun Zhang
Keyword(s):  
Frog Skin ◽  
Trefoil Factor ◽  
Functional Complex ◽  
Skin Secretions

scholarly journals Mosquito repellents in frog skin

2006 ◽  
Vol 2 (2) ◽  
pp. 242-245 ◽  
Author(s):  
C.R Williams ◽  
B.P.C Smith ◽  
S.M Best ◽  
M.J Tyler
Keyword(s):  
Frog Skin ◽  
Volatile Components ◽  
Insect Repellents ◽  
Host Seeking ◽  
Culex Annulirostris ◽  
Litoria Caerulea ◽  
Frog Species ◽  
Mosquito Repellents ◽  
Skin Secretions ◽  
Ectoparasite Infestation

The search for novel insect repellents has been driven by health concerns over established synthetic compounds such as diethyl- m -toluamide (DEET). Given the diversity of compounds known from frog skin and records of mosquito bite and ectoparasite infestation, the presence of mosquito repellents in frogs seemed plausible. We investigated frog skin secretions to confirm the existence of mosquito repellent properties. Litoria caerulea secretions were assessed for mosquito repellency by topical application on mice. The secretions provided protection against host-seeking Culex annulirostris mosquitoes. Olfactometer tests using aqueous washes of skin secretions from L. caerulea and four other frog species were conducted to determine whether volatile components were responsible for repellency. Volatiles from Litoria rubella and Uperoleia mjobergi secretions were repellent to C. annulirostris , albeit not as repellent as a DEET control. The demonstration of endogenous insect repellents in amphibians is novel, and demonstrates that many aspects of frog chemical ecology remain unexplored.

Bm-TFF2, a trefoil factor protein with platelet activation activity from frog Bombina maxima skin secretions

2005 ◽  
Vol 330 (4) ◽  
pp. 1027-1033 ◽  
Author(s):  
Jie Zhang ◽  
Yong Zhang ◽  
Shao-Gui Wan ◽  
Shuang-Shuang Wei ◽  
Wen-Hui Lee ◽  
...  
Keyword(s):  
Platelet Activation ◽  
Trefoil Factor ◽  
Skin Secretions ◽  
Bombina Maxima

scholarly journals Antithrombotics from Frog Skin Secretions

2020 ◽  
Vol 120 (10) ◽  
pp. 1351-1351
Author(s):  
Heyu Ni
Keyword(s):  
Frog Skin ◽  
Skin Secretions

Antitumor and angiostatic peptides from frog skin secretions

Amino Acids ◽  
2010 ◽  
Vol 42 (1) ◽  
pp. 385-395 ◽  
Author(s):  
Hanneke van Zoggel ◽  
Yamina Hamma-Kourbali ◽  
Cécile Galanth ◽  
Ali Ladram ◽  
Pierre Nicolas ◽  
...  
Keyword(s):  
Frog Skin ◽  
Skin Secretions

scholarly journals Different Anti-Candida Activities of Two Human Lactoferrin-Derived Peptides, Lfpep and Kaliocin-1

2005 ◽  
Vol 49 (7) ◽  
pp. 2583-2588 ◽  
Author(s):  
Mónica Viejo-Díaz ◽  
María T. Andrés ◽  
José F. Fierro
Keyword(s):  
Frog Skin ◽  
Fungicidal Activity ◽  
Cytoplasmic Membrane ◽  
Salt Resistance ◽  
Human Lactoferrin ◽  
Striking Similarity ◽  
Homologous Sequence ◽  
Cationic Peptide ◽  
Killing Activity ◽  
Skin Secretions

ABSTRACT The synthetic peptides Lfpep and kaliocin-1 include the sequences from positions 18 to 40 and 153 to 183 of human lactoferrin, respectively. Lfpep is a cationic peptide with bactericidal and giardicidal effects, whereas kaliocin-1 is a novel bactericidal peptide that corresponds to a highly homologous sequence present in the transferrin family of proteins. Both peptides presented fungicidal activity against Candida spp., including fluconazole- and amphotericin B-resistant clinical isolates. Lfpep exhibited higher antifungal activity (8- to 30-fold) and salt resistance than kaliocin-1. The killing activity of Lfpep was mediated by its permeabilizing activity on Candida albicans cells, whereas kaliocin-1 was unable to disrupt the cytoplasmic membrane, as indicated by its inability to allow permeation of propidium iodide and the small amount of K+ released. The amino acid sequence of kaliocin-1 includes the “multidimensional antimicrobial signature” conserved in disulfide-containing antimicrobial peptides and a striking similarity to brevinin-1Sa, an antimicrobial peptide from frog skin secretions, exhibiting a “Rana box”-like sequence. These features may be of interest in the design of new antifungals.

scholarly journals A structural and functional analogue of a Bowman–Birk-type protease inhibitor from Odorrana schmackeri

2017 ◽  
Vol 37 (2) ◽  
Author(s):  
Yuxin Wu ◽  
Qilin Long ◽  
Ying Xu ◽  
Shaodong Guo ◽  
Tianbao Chen ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Frog Skin ◽  
Disulfide Bridge ◽  
Inhibitory Effect ◽  
Skin Secretion ◽  
Drug Discovery And Development ◽  
Trypsin Inhibitory Activity ◽  
Skin Secretions ◽  
Development Pipeline ◽  
First Time

Frog skin secretions contain complex peptidomes and peptidic protease inhibitors that are one of the biologically and structurally described groups of components. In the present study, by use of molecular ‘shotgun’ cloning and LC MS/MS fractionation sequencing, a novel Bowman–Birk-type heptadecapeptide (AALKGCWTKSIPPKPCF-amide), named Odorrana schmackeriTrypsin Inhibitor (OSTI), with a canonical Cys6–Cys16 disulfide bridge, was isolated and identified in piebald odorous frog (O. schmackeri) skin secretion. A synthetic replicate of OSTI-exhibited trypsin inhibitory activity with a Ki value of 0.3 ± 0.04 nM and also a tryptase inhibitory effect with a Ki of 2.5 ± 0.6 μM. This is the first time that this property has been reported for a peptide originating from amphibian sources. In addition, substituting lysine (K) with phenylalanine (F) at the presumed P1 position, completely abrogated the trypsin and tryptase inhibition, but produced a strong chymotrypsin inhibition with a Ki of 1.0 ± 0.1 μM. Thus, the specificity of this peptidic protease inhibitor could be optimized through modifying the amino acid residue at the presumed P1 position and this novel native OSTI, along with its analogue, [Phe9]-OSTI, have expanded the potential drug discovery and development pipeline directed towards alleviation of serine protease-mediated pathologies.

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