Interaction of cyclic and linear Labaditin peptides with anionic and zwitterionic micelles

Barbosa, Simone C.; Cilli, Eduardo Maffud; Dias, Luís Gustavo; Fuzo, Carlos Alessandro; Degrève, Léo; Stábeli, Rodrigo G.; Itri, Rosângela; Ciancaglini, Pietro

doi:10.1016/j.jcis.2014.09.059

Cited by 6 publications

(7 citation statements)

References 62 publications

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“…The band intensity increased with time of adsorption and surface pressure, as it had occurred for the Lo Gibbs monolayer. This result corroborates previous data where the peptide kept its unordered structure even after interacting with LPC and SDS micelles [16], which is due to conformational restrictions of the cyclic peptide. In contrast, Fig.…”

Section: Pm-irras: Secondary Structure and Orientationsupporting

confidence: 92%

“…Changes are associated with the amide I and II bands at 1656 and 1533 cm −1 , respectively, related to the secondary structure of the linear peptide now assuming a major ␣-helix structure upon interacting with S. aureus monolayer. Again, this is consistent with results from the interaction between L 1 and LPC and SDS micelles [16], probably ascribed to the peptide linear structure, which allows L 1 to adopt a different conformation. Castano and co-workers estimated the orientation of ␣-helix peptides at the interfaces when interacting with monolayers through the ratio of the amide I and II band intensities.…”

Section: Pm-irras: Secondary Structure and Orientationsupporting

confidence: 91%

“…Labaditin (Lo) is a small head-to-tail cyclic AMP (VWTVWGTIAG) from Jatropha multifida with high hydrophobic content. In contrast to most of AMPs, it has no charged residues [16,17]. It has been proven effective against Streptococcus mutans, while its linear analogue (L 1 ) is not [17].…”

Section: Introductionmentioning

confidence: 99%

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The importance of cyclic structure for Labaditin on its antimicrobial activity against Staphylococcus aureus

Barbosa

Nobre

Volpati

et al. 2016

Colloids and Surfaces B: Biointerfaces

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Antimicrobial resistance has reached alarming levels in many countries, thus leading to a search for new classes of antibiotics, such as antimicrobial peptides whose activity is exerted by interacting specifically with the microorganism membrane. In this study, we investigate the molecular-level mechanism of action for Labaditin (Lo), a 10-amino acid residue cyclic peptide from Jatropha multifida with known bactericidal activity against Streptococcus mutans. We show that Lo is also effective against Staphylococcus aureus (S. aureus) but this does not apply to its linear analogue (L). Using polarization-modulated infrared reflection absorption spectroscopy (PM-IRRAS), we observed with that the secondary structure of Lo was preserved upon interacting with Langmuir monolayers from a phospholipid mixture mimicking S. aureus membrane, in contrast to L. This structure preservation for the rigid, cyclic Lo is key for the self-assembly of peptide nanotubes that induce pore formation in large unilamellar vesicles (LUVs), according to permeability assays and dynamic light scattering measurements. In summary, the comparison between Labaditin (Lo) and its linear analogue L allowed us to infer that the bactericidal activity of Lo is more related to its interaction with the membrane. It does not require specific metabolic targets, which makes cyclic peptides promising for antibiotics without bacteria resistance.

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Section: Pm-irras: Secondary Structure and Orientationsupporting

confidence: 92%

Section: Pm-irras: Secondary Structure and Orientationsupporting

confidence: 91%

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The importance of cyclic structure for Labaditin on its antimicrobial activity against Staphylococcus aureus

Barbosa

Nobre

Volpati

et al. 2016

Colloids and Surfaces B: Biointerfaces

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“…The solution structure of carnocyclin A was obtained using water as the solvent, while for acidocin B, a membrane-mimicking SDS micelle was employed. Studies have shown that certain peptides undergo conformational changes from a free state in water to a membranebound form in membrane mimetic solvents (52,53,54). The structure of carnocyclin A in water shows that helix 3 is almost perpendicular to helix 1 (17), while helix 1 and 3 of acidocin B are almost parallel.…”

Section: Discussionmentioning

confidence: 99%

Solution Structure of Acidocin B, a Circular Bacteriocin Produced by Lactobacillus acidophilus M46

Acedo

Belkum

Lohans

et al. 2015

Appl Environ Microbiol

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Acidocin B, a bacteriocin produced by Lactobacillus acidophilus M46, was originally reported to be a linear peptide composed of 59 amino acid residues. However, its high sequence similarity to gassericin A, a circular bacteriocin from Lactobacillus gasseri LA39, suggested that acidocin B might be circular as well. Acidocin B was purified from culture supernatant by a series of hydrophobic interaction chromatographic steps. Its circular nature was ascertained by matrix-assisted laser desorption ionizationtime of flight (MALDI-TOF) mass spectrometry and tandem mass spectrometry (MS/MS) sequencing. The peptide sequence was found to consist of 58 amino acids with a molecular mass of 5,621.5 Da. The sequence of the acidocin B biosynthetic gene cluster was also determined and showed high nucleotide sequence similarity to that of gassericin A. The nuclear magnetic resonance (NMR) solution structure of acidocin B in sodium dodecyl sulfate micelles was elucidated, revealing that it is composed of four ␣-helices of similar length that are folded to form a compact, globular bundle with a central pore. This is a three-dimensional structure for a member of subgroup II circular bacteriocins, which are classified based on their isoelectric points of ϳ7 or lower.Comparison of acidocin B with carnocyclin A, a subgroup I circular bacteriocin with four ␣-helices and a pI of 10, revealed differences in the overall folding. The observed variations could be attributed to inherent diversity in their physical properties, which also required the use of different solvent systems for three-dimensional structural elucidation. C ircular bacteriocins are antimicrobial peptides that are ribosomally synthesized by bacteria and are posttranslationally modified to release a leader peptide and form a peptide bond between the N and C termini. These peptides exhibit antimicrobial activity against a broad range of Gram-positive bacteria, including Listeria spp. and Clostridium spp., which are common pathogens causing food-borne diseases (1). In addition, the circular nature of these bacteriocins imparts enhanced stability against proteolytic degradation and denaturation due to extreme temperature and pH conditions relative to linear forms (2). They thus serve as promising alternatives to traditional antimicrobial agents for food, medical, and industrial applications (3).A number of circular bacteriocins that are composed of 58 to 70 amino acid residues have been identified to date, including enterocin AS-48 (4), gassericin A (5), circularin A (6), butyrivibriocin AR10 (7), uberolysin (8), carnocyclin A (9), lactocyclicin Q (10), garvicin ML (11), leucocyclicin Q (12), amylocyclicin (13), and aureocyclicin 4185 (14). Another peptide exhibiting Nto C-terminal cyclization is subtilosin A (15). It is, however, considered a member of the sactipeptides, which represent a class of peptides containing cross-links between cysteine sulfurs and ␣-carbons (16). The structure and genetics of circular bacteriocins were reviewed previously (2). More recently, a re...

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“…Antimicrobial peptides (AMPs) are promising for use against a broad spectrum of antibiotic-resistant bacteria 11–13 , especially as they are capable of disrupting cell membranes 14–18 . Labaditin (Lo), a cyclic decapeptide, head-to-tail, extracted from Jatropha multifida (peptide sequence - VWTVWGTIAG) 19–21 , for instance, has been proven effective against Staphylococcus aureus 22 and Streptococcus mutans 20,21 . Both are Gram-positive, formed by a single lipid bilayer surrounded by a bulky layer of peptidoglycan 23,24 .…”

Section: Introductionmentioning

confidence: 99%

The cyclic peptide labaditin does not alter the outer membrane integrity of Salmonella enterica serovar Typhimurium

Barbosa

Nobre

Volpati

et al. 2019

Sci Rep

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Antimicrobial peptides are a promising class of new antibiotics with the ability to kill bacteria by disrupting their cell membrane, which is especially difficult for Gram-negative bacteria whose cell wall contains an outer layer of lipopolysaccharides (LPS). Here we show that the cyclic decapeptide Labaditin (Lo), with proven activity against the Gram-positive Staphylococcus aureus and Streptococcus mutans, is not able to kill the Gram-negative Salmonella enterica serovar Typhimurium (S.e.s. Typhimurium). We found that Lo induced significant changes in the surface pressure isotherms of Langmuir monolayers representing the Salmonella enterica serovar Typhimurium inner membrane (S.e.s. Typhimurium IM), and caused leakage in large unilamellar vesicles made with this IM lipid composition. On the basis of these results one should expect bactericidal activity against S.e.s. Typhimurium. However, Lo could not interact with a monolayer of LPS, causing no significant changes in either the surface pressure isotherms or in the polarization-modulated infrared reflection absorption spectra (PM-IRRAS). Therefore, the failure of Lo to kill S.e.s. Typhimurium is associated with the lack of interaction with LPS from the outer bacteria membrane. Our approach with distinct monolayer compositions and combined techniques to investigate molecular-level interactions is useful for drug design to fight antibiotic-resistant bacteria.

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Interaction of cyclic and linear Labaditin peptides with anionic and zwitterionic micelles

Cited by 6 publications

References 62 publications

The importance of cyclic structure for Labaditin on its antimicrobial activity against Staphylococcus aureus

The importance of cyclic structure for Labaditin on its antimicrobial activity against Staphylococcus aureus

Solution Structure of Acidocin B, a Circular Bacteriocin Produced by Lactobacillus acidophilus M46

The cyclic peptide labaditin does not alter the outer membrane integrity of Salmonella enterica serovar Typhimurium

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