Vibrational and electronic circular dichroism as powerful tools for the conformational analysis of cationic antimicrobial peptides

Kocourková, Lucie; Novotná, Pavlína; Šťovíčková-Habartová, Lucie; Čujová, Sabína; Čeřovský, Václav; Urbanová, Marie; Setnička, Vladimı́r

doi:10.1007/s00706-016-1807-6

Cited by 8 publications

(6 citation statements)

References 39 publications

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“…There is an amide II band at 1520 cm −1 , and despite being close to a DOPC band, an amide II′ band (for deuterated foldamer) that is clearly distinguishable at 1431 cm −1 on the low‐wavenumber shoulder of the lipid CH 2 bending mode. A combination of amide II and amide II′ bands has been observed before for other peptides embedded in lipid bilayers and possibly occurs due to incomplete hydrogen–deuterium exchange of the amide NH groups ,…”

Section: Resultsmentioning

confidence: 99%

Optically Active Vibrational Spectroscopy of α‐Aminoisobutyric Acid Foldamers in Organic Solvents and Phospholipid Bilayers

Lizio

Andrushchenko

Pike

et al. 2018

Chemistry A European J

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Helical α-aminoisobutyric acid (Aib) foldamers show great potential as devices for the communication of conformational information across phospholipid bilayers, but determining their conformation in bilayers remains a challenge. In the present study, Raman, Raman optical activity (ROA), infrared (IR) and vibrational circular dichroism (VCD) spectroscopies have been used to analyze the conformational preferences of Aib foldamers in solution and when interacting with bilayers. A 3 -helix marker band at 1665-1668 cm in Raman spectra was used to show that net helical content increased strongly with oligomer length. ROA and VCD spectra of chiral Aib foldamers provided the chiroptical signature for both left- and right-handed 3 -helices in organic solvents, with VCD establishing that foldamer screw-sense was preserved when the foldamers became embedded within bilayers. However, the population distribution between different secondary structures was perturbed by the chiral phospholipid. These studies indicate that ROA and VCD spectroscopies are valuable tools for the study of biomimetic structures, such as artificial signal transduction molecules, in phospholipid bilayers.

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Section: Resultsmentioning

confidence: 99%

Optically Active Vibrational Spectroscopy of α‐Aminoisobutyric Acid Foldamers in Organic Solvents and Phospholipid Bilayers

Lizio

Andrushchenko

Pike

et al. 2018

Chemistry A European J

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“…So far, it has been mainly used for the study of α-helical peptides [ 32 , 204 , 207 , 208 ]. Extensions of traditional CD spectroscopy such vibrational and electronic CD also exits as powerful tools for the study of membrane active peptides [ 209 ].…”

Section: Structural Analysismentioning

confidence: 99%

Membrane Active Peptides and Their Biophysical Characterization

2018

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In the last 20 years, an increasing number of studies have been reported on membrane active peptides. These peptides exert their biological activity by interacting with the cell membrane, either to disrupt it and lead to cell lysis or to translocate through it to deliver cargos into the cell and reach their target. Membrane active peptides are attractive alternatives to currently used pharmaceuticals and the number of antimicrobial peptides (AMPs) and peptides designed for drug and gene delivery in the drug pipeline is increasing. Here, we focus on two most prominent classes of membrane active peptides; AMPs and cell-penetrating peptides (CPPs). Antimicrobial peptides are a group of membrane active peptides that disrupt the membrane integrity or inhibit the cellular functions of bacteria, virus, and fungi. Cell penetrating peptides are another group of membrane active peptides that mainly function as cargo-carriers even though they may also show antimicrobial activity. Biophysical techniques shed light on peptide–membrane interactions at higher resolution due to the advances in optics, image processing, and computational resources. Structural investigation of membrane active peptides in the presence of the membrane provides important clues on the effect of the membrane environment on peptide conformations. Live imaging techniques allow examination of peptide action at a single cell or single molecule level. In addition to these experimental biophysical techniques, molecular dynamics simulations provide clues on the peptide–lipid interactions and dynamics of the cell entry process at atomic detail. In this review, we summarize the recent advances in experimental and computational investigation of membrane active peptides with particular emphasis on two amphipathic membrane active peptides, the AMP melittin and the CPP pVEC.

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“…[1][2][3][4][5] It has also been used to resolve the structure of several vital biomolecules. [1][2][3][4][5] It has also been used to resolve the structure of several vital biomolecules.…”

Section: Introductionmentioning

confidence: 99%

“…Inherently structure-sensitive chiroptical spectroscopy is widely used to determine the absolute configuration of pharmaceuticals and to study bioinspired interactions. [1][2][3][4][5] It has also been used to resolve the structure of several vital biomolecules. [6][7][8] Because the structure-function relationship of a molecule is strongly dependent on its natural environment, the analysis of biomolecules directly in biofluids is essential for a deeper insight into many biological processes.…”

Section: Introductionmentioning

confidence: 99%

Electronic circular dichroism for the detection of microalbuminuria

et al. 2018

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Over the past decades, chiroptical spectroscopy has proved its incomparable ability to elucidate the structure and spatial arrangement of chiral molecules. Systematic analysis of biomolecules in the natural environment of biofluids, however, remains challenging. In this study, we used chiroptical spectroscopy to monitor urinary levels of human serum albumin. Not only severe proteinuria but even just a slightly increased urinary excretion of albumin (microalbuminuria) may indicate serious health complications, especially for diabetic individuals. Given the chiral nature of albumin and its typical spectral pattern, it may be easily observable by chiroptical spectroscopy, particularly electronic circular dichroism. The performed chiroptical analysis of urine not only allowed the detection of clinically confirmed microalbuminuria but was also able to reveal this pathological condition in cases beyond the diagnostic capability of common clinical procedures. Thus, our approach suggests that electronic circular dichroism is a useful tool for the fast and reliable qualitative monitoring of microalbuminuria with the potential for a quantitative analysis in the future.

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Vibrational and electronic circular dichroism as powerful tools for the conformational analysis of cationic antimicrobial peptides

Cited by 8 publications

References 39 publications

Optically Active Vibrational Spectroscopy of α‐Aminoisobutyric Acid Foldamers in Organic Solvents and Phospholipid Bilayers

Optically Active Vibrational Spectroscopy of α‐Aminoisobutyric Acid Foldamers in Organic Solvents and Phospholipid Bilayers

Membrane Active Peptides and Their Biophysical Characterization

Electronic circular dichroism for the detection of microalbuminuria

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