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Trichogin GA IV: an antibacterial and protease-resistant peptide
De Zotti, Marta,Biondi, Barbara,Formaggio, Fernando,Toniolo, Claudio,Stella, Lorenzo,Park, Yoonkyung,Hahm, Kyung-Soo John Wiley Sons, Ltd. 2009 Journal of Peptide Science Vol.15 No.9
<P>The antibacterial and hemolytic activities of the amphiphilic helical, membrane-active, lipopeptaibol trichogin GA IV and its [Leu<SUP>11</SUP>-OMe] analogue were compared to those of the partially helical or non-helical 8-meric or 4-meric, C-terminal short sequences, respectively. The study on trichogin GA IV was extended to several methicillin-resistant Staphylococcus aureus strains. Using a large set of enzymes, we also evaluated the resistance to proteolysis of all of the four peptides. Copyright © 2009 European Peptide Society and John Wiley & Sons, Ltd.</P>
Bobone, Sara,Roversi, Daniela,Giordano, Lorenzo,De Zotti, Marta,Formaggio, Fernando,Toniolo, Claudio,Park, Yoonkyung,Stella, Lorenzo American Chemical Society 2012 Biochemistry Vol.51 No.51
<P>Antimicrobial peptides usually kill bacteria by making their membranes permeable. Two main models (barrel-stave and Shai–Matsuzaki–Huang) have been proposed to describe the peptide-induced pores. Although several experimental tests can be exploited to discriminate between these two models, the dependence of peptide activity on lipid properties (intrinsic curvature and membrane thickness) is routinely used for this purpose. Here, we show that, contrary to what is currently accepted, this criterion is unreliable.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/2012/bichaw.2012.51.issue-51/bi3015086/production/images/medium/bi-2012-015086_0004.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/bi3015086'>ACS Electronic Supporting Info</A></P>
Bocchinfuso, Gianfranco,Palleschi, Antonio,Orioni, Barbara,Grande, Giacinto,Formaggio, Fernando,Toniolo, Claudio,Park, Yoonkyung,Hahm, Kyung-Soo,Stella, Lorenzo John Wiley Sons, Ltd. 2009 Journal of peptide science Vol.15 No.9
<P>Most antimicrobial peptides exert their activity by interacting with bacterial membranes, thus perturbing their permeability. They are investigated as a possible solution to the insurgence of bacteria resistant to the presently available antibiotic drugs. However, several different models have been proposed for their mechanism of membrane perturbation, and the molecular details of this process are still debated. Here, we compare fluorescence spectroscopy experiments and molecular dynamics (MD) simulations regarding the association with lipid bilayers and lipid perturbation for two different amphiphilic helical antimicrobial peptides, PMAP-23 and trichogin GA IV. PMAP-23, a cationic peptide member of the cathelicidin family, is considered to induce membrane permeability according to the Shai-Matsuzaki-Huang “carpet” model, while trichogin GA IV is a neutral peptide, member of the peptaibol family. Although several lines of evidence suggest a “barrel-stave” mechanism of pore formation for the latter peptide, its length is only half the normal thickness of a lipid bilayer. Both fluorescence spectroscopy experiments and MD simulations indicated that PMAP-23 associates with membranes close to their surface and parallel to it, and in this arrangement it causes a severe perturbation to the bilayer, both regarding its surface tension and lipid order. By contrast, trichogin GA IV can undergo a transition from a surface-bound state to a transmembrane orientation. In the first arrangement, it does not cause any strong membrane perturbation, while in the second orientation it might be able to span the bilayer from one side to the other, despite its relatively short length, by causing a significant thinning of the membrane. Copyright © 2009 European Peptide Society and John Wiley & Sons, Ltd.</P>
Antonio Paoli,Quirico F. Pacelli,Marco Neri,Luana Toniolo,Pasqua Cancellara,Marta Canato,Tatiana Moro,Marco Quadrelli,Aldo Morra,Diego Faggian,Mario Plebani,Antonino Bianco,Carlo Reggiani 한국식품영양과학회 2015 Journal of medicinal food Vol.18 No.1
Myostatin (MSTN) is a negative regulator of muscle growth even if some studies have shown a counterintuitive positive correlation between MSTN and muscle mass (MM). Our aim was to investigate the influence of 2 months of resistance training (RT) and diets with different protein contents on plasma MSTN, interleukin 1 beta (IL-1b), interleukin 6 (IL-6), tumor necrosis factor alpha (TNF-a), and insulin-like growth factor 1 (IGF-1). Eighteen healthy volunteers were randomly divided in two groups: high protein (HP) and normal protein (NP) groups. Different protein diet contents were 1.8 and 0.85 g of proteinkg bw- 1·day- 1 for HP and NP, respectively. Subjects underwent 8 weeks of standardized progressive RT. MSTN, IGF-1, IL-1b, IL-6, and TNF-a were analyzed before and after the first and the last training sessions. Lean body mass, MM, upper-limb muscle area, and strength were measured. Plasma MSTN showed a significant increase (P < .001) after the last training in the HP group compared with NP group and with starting value. IGF-1 plasma concentration showed a positive correlation with MSTN in HP after the last training (r2 = 0.6456; P = .0295). No significant differences were found between NP and HP for IL-1b, IL-6, TNF-a, and strength and MM or area. These findings suggest a ‘‘paradoxical’’ postexercise increase of plasma MSTN after 8 weeks of RT and HP diets. This MSTN elevation correlates positively with IGF-1 plasma level. This double increase of opposite (catabolic/anabolic) mediators could explain the substantial overlapping of MM increases in the two groups.
Trichogin GA IV: A versatile template for the synthesis of novel peptaibiotics
Zotti, Marta De,Biondi, Barbara,Peggion, Cristina,Formaggio, Fernando,Park, Yoonkyung,Hahm, Kyung-Soo,Toniolo, Claudio The Royal Society of Chemistry 2012 Organic & biomolecular chemistry Vol.10 No.6
<P>Trichogin GA IV, isolated from the fungus <I>Trichoderma longibrachiatum</I>, is the prototype of lipopeptaibols, the sub-class of short-length peptaibiotics exhibiting membrane-modifying properties. This peptaibol is predominantly folded in a mixed 3<SUB>10</SUB>-/α- helical conformation with a clear, albeit modest, amphiphilic character, which is likely to be responsible for its capability to perturb bacterial membranes and to induce cell death. In previous papers, we reported on the interesting biological properties of trichogin GA IV, namely its good activity against Gram positive bacteria, in particular methicillin-resistant <I>S. aureus</I> strains, its stability towards proteolytic degradation, and its low hemolytic activity. Aiming at broadening the antimicrobial activity spectrum by increasing the peptide helical amphiphilicity, in this work we synthesized, by solution and solid-phase methodologies, purified and fully characterized a set of trichogin GA IV analogs in which the four Gly residues at positions 2, 5, 6, 9, lying in the poorly hydrophilic face of the helical structure, are substituted by one (position 2, 5, 6 or 9), two (positions 5 and 6), three (positions 2, 5, and 9), and four (positions 2, 5, 6, and 9) Lys residues. The conformational preferences of the Lys-containing analogs were assessed by FT-IR absorption, CD and 2D-NMR techniques in aqueous, organic, and membrane-mimetic environments. Interestingly, it turns out that the presence of charged residues induces a transition of the helical conformation adopted by the peptaibols (from 3<SUB>10</SUB>- to α-helix) as a function of pH in a reversible process. The role played in the analogs by the markedly increased amphiphilicity was further tested by fluorescence leakage experiments in model membranes, protease resistance, antibacterial and antifungal activities, cytotoxicity, and hemolysis. Taken together, our biological results provide evidence that some of the least substituted among these analogs are good candidates for the development of new membrane-active antimicrobial agents.</P> <P>Graphic Abstract</P><P>One or more Gly-to-Lys replacements on the hydrophilic face of the peptide-template trichogin GA IV modulate its biological properties and promote a pH-mediated, reversible, 3<SUB>10</SUB>- to α-helix transition. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c1ob06178j'> </P>