Conformational properties of the amphipathic lytic polypeptide bombolitin II. A circular dichroism, NMR and computer simulation study

Battistutta, Roberto; Pastore, Annalisa; Mammi, Stefano; Peggion, Evaristo

doi:10.1002/macp.1995.021960909

Cited by 7 publications

(15 citation statements)

References 29 publications

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“…The behaviors of these small membrane peptides are interesting with the comparison of the behavior of the large transmembrane peptides. Among them, Bombolitin II (BLT2), one of the Bombolitins family, has a small size with only 17 amino-acid residues (13)(14)(15)(16)(17)(18)(19)(20)(21). This peptide is hemolytic heptadecapeptides originally isolated from bumblebee venom.…”

Section: Introductionmentioning

confidence: 99%

“…To understand the hemolytic activity of the peptide, elucidation of structure and orientation of BLT2 molecules bound to membranes is certainly important. Battistutta et al (16) performed a computer simulation study of BLT2 that adopts an amphipathic helical structure in a dilute aqueous solution of sodium dodecyl sulfate. The MD simulation of BLT2 was performed by Monticelli et al (20) in a membrane mimetic environment.…”

Section: Introductionmentioning

confidence: 99%

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Molecular Dynamics Simulation of Bombolitin II in the Dipalmitoylphosphatidylcholine Membrane Bilayer

Javkhlantugs

Naito

Ueda

2011

Biophysical Journal

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The orientation behavior of Bombolitin II (BLT2) in the dipalmitoylphosphatidylcholine membrane bilayer was investigated by using molecular-dynamics simulation. During the 20-ns simulation, the BLT2 began to tilt and finally reached the angle of 51° from the membrane-normal. The structure of the peptide formed the amphipathic α-helical structure during the entire simulation time. The peptide tilts with its hydrophobic side faced to the hydrophobic core of the bilayer. We analyzed the mechanism of the tilting behavior of the peptide associated with the membrane in detail. The analysis showed that the hydrogen-bond interaction and the electrostatic interaction were found to exist between Lys(12) and a lipid molecule. These interactions are considered to work as an important factor in tilting the peptide to the membrane-normal.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Molecular Dynamics Simulation of Bombolitin II in the Dipalmitoylphosphatidylcholine Membrane Bilayer

Javkhlantugs

Naito

Ueda

2011

Biophysical Journal

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“…The bombolitins are similar in terms of function and primary structure, especially bombolitins I-III (BLT1-BLT3). It was reported that they assume different secondary structures dependent upon solution conditions such as pH, ionic strength, and peptide concentration [130][131][132], and they adopt predominantly α-helical structure in solutions containing SDS micelles [130,131]. The α-helix in the N-terminal region of BLT3 is stabilized by a salt bridge between Lys2 and Asp5 (residues identical in the sequence of BLT2) at neutral pH [133].…”

Section: Bombolitin IImentioning

confidence: 98%

Recent Solid-State NMR Studies of Membrane-Bound Peptides and Proteins

Naito

Kawamura

Javkhlantugs

2015

Annual Reports on NMR Spectroscopy

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“…The bombolitin family of oligopeptides contains five species with 17-residue sequences derived from bumblebee venom. Their conformations are helical but largely disordered in aqueous solution; in the presence of bilipid membranes, they take on a more ordered, alpha helical structure according to CD studies (19,20). At high concentrations, above 2.5 mM, and in the presence of SDS, the peptides form aggregates (21).…”

Section: Ev)mentioning

confidence: 99%

Peptide secondary structure modulates single-walled carbon nanotube fluorescence as a chaperone sensor for nitroaromatics

Heller

Pratt

Zhang

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

132

138

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A class of peptides from the bombolitin family, not previously identified for nitroaromatic recognition, allows near-infrared fluorescent single-walled carbon nanotubes to transduce specific changes in their conformation. In response to the binding of specific nitroaromatic species, such peptide-nanotube complexes form a virtual "chaperone sensor," which reports modulation of the peptide secondary structure via changes in single-walled carbon nanotubes, near-infrared photoluminescence. A split-channel microscope constructed to image quantized spectral wavelength shifts in real time, in response to nitroaromatic adsorption, results in the first single-nanotube imaging of solvatochromic events. The described indirect detection mechanism, as well as an additional exciton quenching-based optical nitroaromatic detection method, illustrate that functionalization of the carbon nanotube surface can result in completely unique sites for recognition, resolvable at the single-molecule level.bionanotechnology | explosives detection | pesticides | spectroscopy | optical sensors S ingle-walled carbon nanotubes (SWNT) emit near-infrared (NIR) bandgap photoluminescence (PL) (1, 2), which is highly responsive to its physical and chemical environment (3-6). SWNT are unique among nanoscale sensor platforms in their ability to detect the adsorption of as few as a single molecule of an analyte (7,8). For such a capability to be extended to specific classes of organic molecules, chemical approaches must be developed that allow for selective molecular recognition. Stepwise quenching of SWNT PL by single-molecule adsorption events to the nanotube surface (7) has been demonstrated (8, 9). Our previous findings extend this resolution to biologically important reactive oxygen species and demonstrate multiplexed detection of redox-active analytes by two optical modes, leading to species identification (9).The current work investigates the selective optical detection of binding events by single-SWNT PL modulation, employing both intensity-and wavelength-based signal transduction. We find that specific noncovalently bound polymers can be harnessed to change the properties of the nanotube-polymer complex, resulting in complete modulation of the nanotube sensitivity to certain analytes. Resolution of an entire class of molecules can be achieved by the nanotube via reporting the conformational state of a peptide, for example. Nanotube emission undergoes solvatochromic shifts due to nitroaromatic compound-mediated secondary structure changes of the amphipathic bombolitin II oligopeptide. In this work, we probe solvatochromic interactions at the single-nanotube level by a strategy in which two spectrally adjacent optical channels measure anticorrelated, quantized fluctuations, signifying molecular binding events. In addition, we find that an oligonucleotide of single-stranded DNA with the sequence ðATÞ 15 [ssðATÞ 15 ] oligonucleotide imparts optical selectivity of SWNT for trinitrotoluene (TNT) via intensity modulation. Although nanotubes do not ...

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Conformational properties of the amphipathic lytic polypeptide bombolitin II. A circular dichroism, NMR and computer simulation study

Cited by 7 publications

References 29 publications

Molecular Dynamics Simulation of Bombolitin II in the Dipalmitoylphosphatidylcholine Membrane Bilayer

Molecular Dynamics Simulation of Bombolitin II in the Dipalmitoylphosphatidylcholine Membrane Bilayer

Recent Solid-State NMR Studies of Membrane-Bound Peptides and Proteins

Peptide secondary structure modulates single-walled carbon nanotube fluorescence as a chaperone sensor for nitroaromatics

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