Orientation of the benzophenone group at various depths in bilayers

Lala, Anil K.; Kumar, Erukulla Ravi

doi:10.1021/ja00063a018

Cited by 21 publications

(21 citation statements)

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“…The kinetics of hydrogen abstraction by the benzophenone triplet is directly related to the number of secondary, allylic, and doubly allylic hydrogen atoms in the phospholipid molecule, as follows: k H ={0.023[H sec ]+0.112[H allylic ]+1.78[H doubly allylic ]}×10 7 m −1 s −1 . The cross‐linking is not restricted to a single carbon atom, but covers a broad range of 5–6 carbon atoms along the acyl chain . Furthermore, the range of functionalized carbon atoms is centered at the position expected from the transverse location of the benzophenone‐modified phospholipid in the bilayer …”

Section: Methodsmentioning

confidence: 99%

“…The cross‐linking is not restricted to a single carbon atom, but covers a broad range of 5–6 carbon atoms along the acyl chain . Furthermore, the range of functionalized carbon atoms is centered at the position expected from the transverse location of the benzophenone‐modified phospholipid in the bilayer …”

Section: Methodsmentioning

confidence: 99%

“…We assumed that if benzophenone behavior in penetratin strictly conforms to that of the free probe, the reactivity of photoactivatable penetratin with saturated and unsaturated phospholipids should strictly rely on the kinetics of hydrogen abstraction (Scheme ) . We calculated this reactivity for the different phospholipids in Table by estimating the number of possible cross‐linking positions in the acyl chains as a mean of 5–6 carbon atoms …”

Section: Methodsmentioning

confidence: 99%

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Exploiting Benzophenone Photoreactivity To Probe the Phospholipid Environment and Insertion Depth of the Cell‐Penetrating Peptide Penetratin in Model Membranes

et al. 2017

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Penetratin (RQIKIWFQNRRMKWKK) enters cells by different mechanisms, including membrane translocation, thus implying that the peptide interacts with the lipid bilayer. Penetratin also crosses the membrane of artificial vesicles, depending on their phospholipid content. To evaluate the phospholipid preference of penetratin, as the first step of translocation, we exploited the benzophenone triplet kinetics of hydrogen abstraction, which is slower for secondary than for allylic hydrogen atoms. By using multilamellar vesicles of varying phospholipid content, we identified and characterized the cross‐linked products by MALDI‐TOF mass spectrometry. Penetratin showed a preference for negatively charged (vs. zwitterionic) polar heads, and for unsaturated (vs. saturated) and short (vs. long) saturated phospholipids. Our study highlights the potential of using benzophenone to probe the environment and insertion depth of membranotropic peptides in membranes.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Exploiting Benzophenone Photoreactivity To Probe the Phospholipid Environment and Insertion Depth of the Cell‐Penetrating Peptide Penetratin in Model Membranes

et al. 2017

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“…These acyl chains being saturated or transunsaturated are indeed found in more packed membrane domains (see main transition temperatures given in the Experimental section). In addition, although DLoPG should give the fastest kinetics thanks to the doubly allylic H • abstraction 18 (Figure S8), the corresponding photoadduct (Pen-LoA) has the lowest intensity signal relative to the one of Pen (Figure 2). This is likely due to the low stability of the formed adduct compared to other acyl chains, as supported by tandem mass spectrometry (MS/MS; Figure S10) data that have been discussed above.…”

Section: New Insights In Pen Preference For Fluid-phase Bilayersmentioning

confidence: 99%

Benzophenone Photoreactivity in a Lipid Bilayer To Probe Peptide/Membrane Interactions: Simple System, Complex Information

et al. 2019

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Affinity photocrosslinking coupled to mass spectrometry, using benzophenone (Bzp)-functionalized peptides, was used to study the non-covalent interactions of cell-penetrating peptides and lipid membranes. Using biomimetic lipid vesicles composed of saturated and unsaturated negatively charged lipids: DMPG (14:0), DPPG (16:0), DOPG (18:1 cis Δ 9), 18:1 (trans Δ 9) PG and DLoPG (18:2 cis Δ 9, 12), allowed to observe all the classical and less common reactivities of Bzp described in the literature by direct MS analysis: C=C double bond formation on saturated fatty acids, covalent adducts formation via classical CC bond and Paternò-Büchi oxetane formation followed or not by fragmentation (retro-Paternò-Büchi) as well as photosensitisation of unsaturated lipids leading to lipid dimers. All these reactions can occur concomitantly in a single complex biological system: a membrane-active peptide inserted within a phospholipid bilayer. We also detect oxidation species due to the presence of radical oxygen species. This work represents a noteworthy improvement for the characterisation of interacting partners using Bzp photocrosslinking, and shows how to exploit in an original way the different reactivities of Bzp in the context of a lipid membrane. We propose an analytical workflow for the interpretation of MS spectra, giving access to information on the CPP/lipid interaction at a molecular level such as depth of insertion or membrane fluidity in the CPP vicinity. An application of this workflow illustrates the role of cholesterol in the CPP/lipids interaction. Supporting information Available Detailed experimental procedures and (R/W)9 results are given in the Supporting Information.

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“…[7] Thec ross-linking is not restricted to as ingle carbon atom, but covers ab road range of 5-6 carbon atoms along the acyl chain. [8] Furthermore,the range of functionalized carbon atoms is centered at the position expected from the transverse location of the benzophenone-modified phospholipid in the bilayer. [8] In this study,b enzophenone photolabeling (Scheme 1) was used to examine whether penetratin can recruit particular phospholipids in membranes.T he benzophenone moiety was Scheme 1.…”

mentioning

confidence: 99%

Exploiting Benzophenone Photoreactivity To Probe the Phospholipid Environment and Insertion Depth of the Cell‐Penetrating Peptide Penetratin in Model Membranes

et al. 2017

View full text Add to dashboard Cite

Penetratin (RQIKIWFQNRRMKWKK) enters cells by different mechanisms, including membrane translocation, thus implying that the peptide interacts with the lipid bilayer. Penetratin also crosses the membrane of artificial vesicles, depending on their phospholipid content. To evaluate the phospholipid preference of penetratin, as the first step of translocation, we exploited the benzophenone triplet kinetics of hydrogen abstraction, which is slower for secondary than for allylic hydrogen atoms. By using multilamellar vesicles of varying phospholipid content, we identified and characterized the cross-linked products by MALDI-TOF mass spectrometry. Penetratin showed a preference for negatively charged (vs. zwitterionic) polar heads, and for unsaturated (vs. saturated) and short (vs. long) saturated phospholipids. Our study highlights the potential of using benzophenone to probe the environment and insertion depth of membranotropic peptides in membranes.

show abstract

Orientation of the benzophenone group at various depths in bilayers

Cited by 21 publications

References 1 publication

Exploiting Benzophenone Photoreactivity To Probe the Phospholipid Environment and Insertion Depth of the Cell‐Penetrating Peptide Penetratin in Model Membranes

Exploiting Benzophenone Photoreactivity To Probe the Phospholipid Environment and Insertion Depth of the Cell‐Penetrating Peptide Penetratin in Model Membranes

Benzophenone Photoreactivity in a Lipid Bilayer To Probe Peptide/Membrane Interactions: Simple System, Complex Information

Exploiting Benzophenone Photoreactivity To Probe the Phospholipid Environment and Insertion Depth of the Cell‐Penetrating Peptide Penetratin in Model Membranes

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