β-Sheet Structures and Dimer Models of the Two Major Tyrocidines, Antimicrobial Peptides fromBacillus aneurinolyticus

Biochemistry ◽  
2013 ◽  
Vol 52 (44) ◽  
pp. 7798-7806 ◽  
Author(s):  
Gadzikano Munyuki ◽  
Graham E. Jackson ◽  
Gerhard A. Venter ◽  
Katalin E. Kövér ◽  
László Szilágyi ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Β Sheet ◽  
Dimer Models

scholarly journals Short Synthetic β-Sheet Antimicrobial Peptides for the Treatment of Multidrug-ResistantPseudomonas aeruginosaBurn Wound Infections

2017 ◽  
Vol 6 (7) ◽  
pp. 1601134 ◽  
Author(s):  
Guansheng Zhong ◽  
Junchi Cheng ◽  
Zhen Chang Liang ◽  
Liang Xu ◽  
Weiyang Lou ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Wound Infections ◽  
Β Sheet

scholarly journals Characterization of Four Liver-Expressed Antimicrobial Peptides from Antarctic Fish and Their Antibacterial Activity

2019 ◽  
Vol 9 (20) ◽  
pp. 4299 ◽  
Author(s):  
Shweta Borkar ◽  
Sondavid Nandanwar ◽  
Jun Lee ◽  
Hak Kim
Keyword(s):  
Antibacterial Activity ◽  
Antimicrobial Peptides ◽  
Antarctic Fish ◽  
Effect Of Temperature ◽  
Dissostichus Mawsoni ◽  
Sytox Green ◽  
Uptake Assay ◽  
The Antarctic ◽  
Β Sheet

Liver-expressed antimicrobial peptides (LEAPs) are cysteine-containing cationic peptides. LEAP-1 and LEAP-2 are eight- and four-cysteine containing antimicrobial peptides found in animals, respectively. LEAP-1 is widely known as antibacterial peptide involved in the innate immunity of fish, but the roles of LEAP-1 and LEAP-2 in Antarctic fish species are unknown. In the present study, we synthesized and characterized novel LEAPs with four and eight cysteine residues, derived from Antarctic notothenioid (Dissostichus mawsoni) and Antarctic eelpout (Lycodichthys dearborni). Circular dichroism spectroscopy of these peptides showed a typical β-sheet conformation. The LEAPs were found to be bactericidal against gram-positive as well as gram-negative bacteria. In the SYTOX green uptake assay, LEAPs did not trigger any significant increase in fluorescence. However, LEAPs competitively bound to DNA and replaced the ethidium bromide (EB) dye. To determine the effect of temperature on the activity of LEAPs, we evaluated the antibacterial activity against Listeria monocytogenes at 5, 15, 25, and 35 °C. The results showed that the antibacterial activity of LEAPs increased with a decrease in temperature, which may indicate that the Antarctic fish LEAP are evolutionarily adapted. Taken together, our results suggest that novel Antarctic LEAPs are bactericidal peptides with the likely mode of action being DNA binding and may be evolved to adapt to cold temperature.

scholarly journals Antimicrobial Activities and Structures of Two Linear Cationic Peptide Families with Various Amphipathic β-Sheet and α-Helical Potentials

2005 ◽  
Vol 49 (12) ◽  
pp. 4957-4964 ◽  
Author(s):  
Yi Jin ◽  
Janet Hammer ◽  
Michelle Pate ◽  
Yu Zhang ◽  
Fang Zhu ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Antimicrobial Peptides ◽  
Plasma Membranes ◽  
Membrane Lipids ◽  
Lipid Vesicles ◽  
Selective Advantage ◽  
Antimicrobial Activities ◽  
Helical Conformation ◽  
Bacterial Cells ◽  
Β Sheet

ABSTRACT Many naturally occurring antimicrobial peptides comprise cationic linear sequences with the potential to adopt an amphipathic α-helical conformation. We designed a linear 18-residue peptide that adopted an amphipathic β-sheet structure when it was bound to lipids. In comparison to a 21-residue amphipathic α-helical peptide of equal charge and hydrophobicity, this peptide possessed more similar antimicrobial activity and greater selectivity in binding to and inducing leakage in vesicles composed of bacterial membrane lipids than vesicles composed of mammalian membrane lipids (J. Blazyk, R. Weigand, J. Klein, J. Hammer, R. M. Epand, R. F. Epand, W. L. Maloy, and U. P. Kari, J. Biol. Chem. 276:27899-27906, 2001). Here, we compare two systematically designed families of linear cationic peptides to evaluate the importance of amphipathicity for determination of antimicrobial activity. Each peptide contains six lysine residues and is amidated at the carboxyl terminus. The first family consists of five peptides with various capacities to form amphipathic β-sheet structures. The second family consists of six peptides with various potentials to form amphipathic α helices. Only those peptides that can form a highly amphipathic structure (either a β sheet or an α helix) possessed significant antimicrobial activities. Striking differences in the abilities to bind to and induce leakage in membranes and lipid vesicles were observed for the two families. Overall, the amphipathic β-sheet peptides are less lytic than their amphipathic α-helical counterparts, particularly toward membranes containing phosphatidylcholine, a lipid commonly found in mammalian plasma membranes. Thus, it appears that antimicrobial peptides that can form an amphipathic β-sheet conformation may offer a selective advantage in targeting bacterial cells.

scholarly journals USING SEQUENCE PATTERNS TO IDENTIFY AND DESIGN NEW ANTIMICROBIAL PEPTIDES

2019 ◽  
Vol 19 (1S) ◽  
pp. 162-164
Author(s):  
I E Eliseev ◽  
I N Terterov ◽  
O V Shamova
Keyword(s):  
Antimicrobial Peptides ◽  
Synthetic Peptides ◽  
Comprehensive Analysis ◽  
Characteristic Sequence ◽  
Natural Antimicrobial ◽  
Sequence Patterns ◽  
Sheet Structure ◽  
Functional Features ◽  
Computational Identification ◽  
Β Sheet

Natural antimicrobial peptides (AMPs) are remarkably diverse, yet they all share some common structural and functional features. In an attempt to find what determines similar activities of non-homologous molecules, we performed a comprehensive analysis of sequence patterns in AMPs. We found that natural AMPs possess characteristic sequence patterns, and these patterns differ for peptides with α-helical and β-sheet structure. We showed that the patterns facilitate computational identification of AMPs in databases. We then used patterns to design new peptides, synthesized them and assayed for antibacterial activity. The most active among synthetic peptides exhibited activity against Gram(+) and Gram(-) pathogens comparable to best natural AMPs.

scholarly journals Refinement of the Fusion Tag PagP For Efficient Inclusion Body-Targeted Expression of Recombinant Antimicrobial Peptides in Escherichia Coli

2021 ◽  
Author(s):  
Xuefeng Li ◽  
Baorong Zhang ◽  
Quan Hu ◽  
Changchao Chen ◽  
Lu Liu ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Inclusion Body ◽  
Fusion Partner ◽  
Separation And Purification ◽  
Linker Peptide ◽  
Dense Distribution ◽  
Targeted Expression ◽  
Magainin Ii ◽  
Β Sheet

Abstract The methods developed for efficient insoluble protein production are less well explored. Our data demonstrated that PagP, an E. coli outer membrane protein with high β-sheet content, could function as an efficient fusion partner for inclusion body-targeted expression of antimicrobial peptide Magainin II, Metchnikowin and Andropin. The primary structure of a given polypeptide determines to a large extent its propensity to aggregate. The aggregation “hot spots” (HSs) in PagP was subsequently analyzed with the web-based software AGGRESCAN, leading to identification of the C-terminal region with high dense distribution of HSs. The absolute yields of recombinant antimicrobial peptide Metchnikowin and Andropin could be increased significantly when expressed in fusion with this version of PagP. Moreover, a Proline-rich region was found in the β-strands of PagP. Substitution for these prolines by residues with high β-sheet propensity and hydrophobicity significantly improved its ability to form aggregates, and greatly increased the yield of the recombinant passenger peptides. Fewer examples have been presented to separate the recombinant target proteins expressed in fusion inclusion bodies. Here, we reported an artificial linker peptide NHT with three motifs, by which separation and purification of the authentic recombinant antimicrobial peptides could be implemented.

Measuring the Binding of an Antimicrobial Peptide with LPS by Fluoresence Correlation Spectroscopy

2012 ◽  
Author(s):  
Lanlan Yu ◽  
Ling Ding Jeak ◽  
Thorsten Wohland
Keyword(s):  
Antimicrobial Peptides ◽  
Fluorescence Correlation Spectroscopy ◽  
Computational Models ◽  
Correlation Spectroscopy ◽  
New Drugs ◽  
Microbial Diseases ◽  
Fluorescence Correlation ◽  
Β Sheet ◽  
Lipid Interaction

Antimicrobial peptides are an important defense weapon of many organisms, which attack the membrane of bacteria, leading to inhibition of bacterial growth and finally, bacterial death. Despite their ancient origin, it is difficult for bacteria to develop resistance against these peptides. This makes antimicrobial peptides a promising candidate for new drugs against microbial diseases. The target of these peptides is lipopolysaccharides (LPS), which are the major component of the outer membrane of Gram–negative bacteria. Known peptide structures and computational models show an amphipathic cationic pattern BHPHB (B: basic; H: hydrophobic; P: polar residue, respectively), which is the possible binding site of antimicrobial peptides to LPS. A cyclic amphipathic cationic 19–residue peptide (V4) with one disulfide bond has been designed (Frecer et al., unpublished data), which has potential antimicrobial activity. Circular dichroism measurements showed that V4 has a β–sheet structure. The interaction of a fluorophore labeled–V4 with LPS has been investigated by fluorescence correlation spectroscopy (FCS). The study demonstrated that V4 can specifically bind LPS, in contrast to zwitterionic phosphatidylcholine (PC) of eukaryotic cells. FCS makes it possible to study the binding between peptide and LPS at low concentration in vitro. The dissociation constant of the peptide and LPS was obtained using this technique. Key words: antimicrobial peptides, LPS, peptide-lipid interaction, fluorescence correlation spectroscopy

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