Three-dimensional structure of the ion-chanel forming peptide trichorzianin TA VII bound to sodium dodecyl sulfate micelles

Condamine, Eric; Rebuffat, Sylvie; Prigent, Yann; Ségalas, Isabelle; Bodo, Bernard; Davoust, Daniel

doi:10.1002/(sici)1097-0282(199808)46:2<75::aid-bip3>3.0.co;2-u

Cited by 18 publications

(5 citation statements)

References 57 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…the conformations are similar to the structure observed for chrysospermin C in terms of bend angle and atomic coordinates [46]. Recently, a NMR solution structure in SDS micelles for trichorzianin A VII, another long peptaibol which forms voltage‐dependent channels, has been reported [9]. Two structural families exhibiting a bend angle of 90–100° between two well‐defined N‐terminal and C‐terminal right‐handed α‐helices were found [9].…”

Section: Discussionsupporting

confidence: 52%

“…Recently, a NMR solution structure in SDS micelles for trichorzianin A VII, another long peptaibol which forms voltage‐dependent channels, has been reported [9]. Two structural families exhibiting a bend angle of 90–100° between two well‐defined N‐terminal and C‐terminal right‐handed α‐helices were found [9]. With this bend angle, a single molecule could not span a membrane bilayer.…”

Section: Discussionmentioning

confidence: 99%

“…Preliminary NMR experiments indicated that at these peptide/dodecylphosphocholine ratios the peptide is monomeric as no further change in the NMR spectrum was observed for peptide/dodecylphosphocholine ratios up to 1 : 100. Previous NMR structure determinations of peptides in lipid micelles were carried out at temperatures between 25 and 40 °C [5–15]. There was very little variation in the NMR spectrum of chrysospermin C over 25–50 °C and a temperature of 45 °C, which resulted in an average amide line width of 8.6 Hz, was therefore used in all experiments.…”

Section: Methodsmentioning

confidence: 99%

“…Because this suggested that a membrane or membrane‐like environment is probably a prerequisite for formation of a stably folded conformation of chrysospermin C, we extended our previous work to study chrysospermin C bound to dodecylphosphocholine micelles. Although micelles are not a perfect mimic of lipid bilayers, a substantial number of structural determinations for peptides and proteins bound to micelles have indicated that valuable structural information can be obtained from NMR studies of such systems [5–15].…”

mentioning

confidence: 99%

See 3 more Smart Citations

The NMR solution structure of the ion channel peptaibol chrysospermin C bound to dodecylphosphocholine micelles

Anders¹,

Ohlenschläger²,

Šoškić³

et al. 2000

European Journal of Biochemistry

View full text Add to dashboard Cite

Chrysospermin C is a 19-residue peptaibol capable of forming transmembrane ion channels in phospholipid bilayers. The conformation of chrysospermin C bound to dodecylphosphocholine micelles has been solved using heteronuclear NMR spectroscopy. Selective 15N-labeling and 13C-labeling of specific alpha-aminoisobutyric acid residues was used to obtain complete stereospecific assignments for all eight alpha-aminoisobutyric acid residues. Structures were calculated using 339 distance constraints and 40 angle constraints obtained from NMR data. The NMR structures superimpose with mean global rmsd values to the mean structure of 0. 27 A (backbone heavy atoms) and 0.42 A (all heavy atoms). Chrysospermin C bound to decylphosphocholine micelles displays two well-defined helices at the N-terminus (residues Phe1-Aib9) and C-terminus (Aib13-Trp-ol19). A slight bend preceding Pro14, i.e. encompassing residues 10-12, results in an angle of approximately 38 degrees between the mean axes of the two helical regions. The bend structure observed for chrysospermin C is compatible with the sequences of all 18 long peptaibols and may represent a common 'active' conformation. The structure of chrysospermin C shows clear hydrophobic and hydrophilic surfaces which would be appropriate for the formation of oligomeric ion channels.

show abstract

Section: Discussionsupporting

confidence: 52%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

The NMR solution structure of the ion channel peptaibol chrysospermin C bound to dodecylphosphocholine micelles

Anders¹,

Ohlenschläger²,

Šoškić³

et al. 2000

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…Peptaibols show antibiotic properties by forming pores within biological membranes via aggregation, the implication of which has been widely studied [10,11,12]. Apart from studies on their bioactivity, substantial focus has been given to their three-dimensional structures and folding dynamics [13,14,15,16]. In the protein databank (PDB, ) about 15 experimentally (X-ray crystallography or NMR) known structures have been documented so far.…”

Section: Introductionmentioning

confidence: 99%

Tripleurin XIIc: Peptide Folding Dynamics in Aqueous and Hydrophobic Environment Mimic Using Accelerated Molecular Dynamics

et al. 2019

View full text Add to dashboard Cite

Peptaibols are a special class of fungal peptides with an acetylated N-terminus and a C-terminal 1,2-amino alcohol along with non-standard amino acid residues. New peptaibols named tripleurins were recently identified from a strain of the filamentous fungal species Trichoderma pleuroti, which is known to cause green mould disease on cultivated oyster mushrooms. To understand the mode of action of these peptaibols, the three-dimensional structure of tripleurin (TPN) XIIc, an 18-mer peptide, was elucidated using an enhanced sampling method, accelerated MD, in water and chloroform solvents. Non-standard residues were parameterized by the Restrained Electrostatic Potential (RESP) charge fitting method. The dihedral distribution indicated towards a right-handed helical formation for TPN XIIc in both solvents. Dihedral angle based principal component analysis revealed a propensity for a slightly bent, helical folded conformation in water solvent, while two distinct conformations were revealed in chloroform: One that folds into highly bent helical structure that resembles a beta-hairpin and another with an almost straight peptide backbone appearing as a rare energy barrier crossing event. The hinge-like movement of the terminals was also observed and is speculated to be functionally relevant. The convergence and efficient sampling is addressed using Cartesian PCA and Kullback-Leibler divergence methods.

show abstract

NMR of Membrane‐Associated Peptides and Proteins

Bader

Lerch

Zerbe

2008

Protein Science Encyclopedia

View full text Add to dashboard Cite

Originally published in: BioNMR in Drug Research. Edited by Oliver Zerbe. Copyright © 2002 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30465‐7 The sections in this article are The Biochemistry of Membrane Interactions Introduction Biological Membranes Protein‐Membrane Interactions Aggregate Structures of Lipids and their Biophysics Micelles Bicelles Vesicles or Liposomes The NMR Sample Synthesis of Peptides and Proteins Choice of Detergent Choice of pH Choice of Temperature Salt Concentrations Practical Tips for Sample Preparation The Structure and Dynamics of Membrane‐Associated Peptides – A Case Study of Neuropeptide Y ( NPY ) Introduction Structure Determination of Micelle‐Bound NPY The Determination of the Topology of the Membrane‐ NPY Interface Spin Labels Amide H , D Exchange Measurement of Internal Dynamics of NPY / DPC

show abstract

Three-dimensional structure of the ion-chanel forming peptide trichorzianin TA VII bound to sodium dodecyl sulfate micelles

Cited by 18 publications

References 57 publications

The NMR solution structure of the ion channel peptaibol chrysospermin C bound to dodecylphosphocholine micelles

The NMR solution structure of the ion channel peptaibol chrysospermin C bound to dodecylphosphocholine micelles

Tripleurin XIIc: Peptide Folding Dynamics in Aqueous and Hydrophobic Environment Mimic Using Accelerated Molecular Dynamics

NMR of Membrane‐Associated Peptides and Proteins

Contact Info

Product

Resources

About