Electric field influence on the helical structure of peptides: insights from DFT/PCM computations

Ilieva, Sylvia; Cheshmedzhieva, Diana; Dudev, Todor

doi:10.1039/c9cp01542f

Cited by 9 publications

(9 citation statements)

References 60 publications

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“…Notably, a single FF nanostructure possesses a spontaneous dipole moment that can be switched by an electric field due to their helix structures (Figure 1c). [ 35,36 ] Because the electronegativity of the oxygen atom is relatively higher than that of the hydrogen atom, the carboxylic acid group (COO − ) of FF molecules becomes a proton and strongly interacts with the amine group (NH 3 + ) of other FF molecules via hydrogen bonding, making it possible to get the electric dipole moment pointing from COO − to NH 3 + . Furthermore, the self‐assembled FF nanostructure remains an α‐helix structure; thus, there is a spontaneous polarization along the axial direction of the structure, which arises from the orientation ordering of hydrogen bonds.…”

Section: Resultsmentioning

confidence: 99%

Large‐Scale Assembly of Peptide‐Based Hierarchical Nanostructures and Their Antiferroelectric Properties

Lee

Kim

Duong

et al. 2020

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organized structures enable the expression of completely different physical properties, which are absent in the basic material, and endow many biological materials with remarkable mechanical strength, [4] flexibility, [5] super-hydrophobicity, [6] and optical properties, [7] such as structural color. Therefore, many researchers have made great efforts to develop novel materials with unique physical properties and improved performance over conventional materials by mimicking these natural hierarchical structures. Although various biomaterials, such as DNA, [8] bacteriophages, [9] proteins, [10] carbohydrates, [11] and peptides, [12] are being researched and developed for this purpose, self-assembled peptide nanostructures [13] are most actively studied among them owing to their versatile properties. Diphenylalanine (FF) molecules, especially those derived from the dipeptide motif (-F19-F20-), which is a major contributing factor in amyloid fibril formation that causes Alzheimer's disease, are widely used to form peptide hierarchical nanostructures through a self-assembly process that induces the aggregation of FF molecules in water. [14] This molecular self-assembly approach enables us to build diverse peptide nanostructures with functional physical and chemical properties, including piezoelectricity, [15] ferroelectricity, [16] and photoluminescence, [17] as well as robust An effective strategy is developed to create peptide-based hierarchical nanostructures through the meniscus-driven self-assembly in a large area and fabricate antiferroelectric devices based on these nanostructures for the first time. The diphenylalanine hierarchical nanostructures (FF-HNs) are self-assembled by vertically pulling a substrate from a diphenylalanine (FF) solution dissolved in a miscible solvent under precisely controlled conditions. Owing to the unique structural properties of FF nanostructures, including high crystallinity and α-helix structures, FF-HNs possess a net electrical dipole moment, which can be switched in an external electric field. The mass production of antiferroelectric devices based on FF-HNs can be successfully achieved by means of this biomimetic assembly technique. The devices show an evident antiferroelectric to ferroelectric transition under dark conditions, while the ferroelectricity is found to be tunable by light. Notably, it is discovered that the modulation of antiferroelectric behaviors of FF-HNs under glutaraldehyde exposure is due to the FF molecules that are transformed into cyclophenylalanine by glutaraldehyde. This work provides a stepping stone toward the mass production of self-assembled hierarchical nanostructures based on biomolecules as well as the mass fabrication of electronic devices based on biomolecular nanostructures for practical applications.

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Section: Resultsmentioning

confidence: 99%

Large‐Scale Assembly of Peptide‐Based Hierarchical Nanostructures and Their Antiferroelectric Properties

Lee

Kim

Duong

et al. 2020

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“…Dudev and co-workers examined the effect of static EFs on the secondary structure of a range of model helical peptides. 45 These authors found that application of intense external fields (>2.5 V nm −1 ) along the axis of the helix resulted in the loss of helical structure and formation of unusual cyclic/ring peptide conformations. 45 Dudev and co-workers also examined the impact of external EFs on a model salt-bridge peptide, finding minimal disruption of the underling Lys-Asp pair at the field strengths and orientations studied.…”

Section: Recent Case Studiesmentioning

confidence: 99%

“…45 These authors found that application of intense external fields (>2.5 V nm −1 ) along the axis of the helix resulted in the loss of helical structure and formation of unusual cyclic/ring peptide conformations. 45 Dudev and co-workers also examined the impact of external EFs on a model salt-bridge peptide, finding minimal disruption of the underling Lys-Asp pair at the field strengths and orientations studied. 45 While these authors noted that these EF-induced perturbations of secondary structure were reversible, 45 we should emphasise the peptides were considered in isolation.…”

Section: Recent Case Studiesmentioning

confidence: 99%

Electromagnetic bioeffects: a multiscale molecular simulation perspective

Noble

Todorova

Yarovsky

2022

Phys. Chem. Chem. Phys.

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“…Electric fields are able to induce cleavage and formation of covalent bonds [1]. It has been shown that oriented external electric fields (OEEF) have considerable effects on DNA mutation [2, 3], helical structure of peptides [4], and can tune the reactivity of NH 3 ⋯HCl/H 2 O acid–base pairs [5] and formic acid dimers [6]. Electric fields have been used also to catalyze the molecular hydrogen formation from simple alcohols [7] or for catalyzing fundamental proton transfer reactions [8].…”

Section: Introductionmentioning

confidence: 99%

Effect of external electric field on the tautomeric equilibrium and structure of 2‐carbamido‐1,3‐indandione

Enchev

Маркова

2021

Int J of Quantum Chemistry

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2‐Carbamido‐1,3‐indandione (CAID) is a new reliable fluorescent biomarker and it exists in two tautomeric forms: 2‐(hydroxyl‐aminomethylidene)‐indan‐1,3‐dione (A) and 2‐carboamide‐1‐hydroxy‐3‐oxo‐indan (B). The structures of the tautomers and the transition state for intramolecular proton transfer are located at MP2/6‐31+G(d) level for each magnitude and for opposite directions of the applied electric field. According to our SCS‐MP2/6‐31+G(d) field‐free calculations tautomer A prevails (59.3%) while variation of the electric field strength along the direction from the indandione moiety to the carbamido fragment (+x‐direction) leads to stabilization of tautomer B. The two tautomeric forms become isoenergetic at 2.571 V/Å when the applied electric field is parallel to the direction from amino to the hydroxyl group (−y‐direction) in CAID, and at 3.085 V/Å tautomer B (51.9%) is slightly favored. Apparently, an external electric field has a strong influence on the tautomeric equilibrium in the CAID molecule.

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Electric field influence on the helical structure of peptides: insights from DFT/PCM computations

Abstract: The switching of the electric field with a particular directionality could be used for the healing of misfolded proteins.

Cited by 9 publications

References 60 publications

Large‐Scale Assembly of Peptide‐Based Hierarchical Nanostructures and Their Antiferroelectric Properties

Large‐Scale Assembly of Peptide‐Based Hierarchical Nanostructures and Their Antiferroelectric Properties

Electromagnetic bioeffects: a multiscale molecular simulation perspective

Effect of external electric field on the tautomeric equilibrium and structure of 2‐carbamido‐1,3‐indandione

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