Structure and dynamics of lipid‐associated states of apocytochrome <i>c</i>

Bryson, Elzbieta A; Rankin, Saffron E.; Goormaghtigh, Erik; Ruysschaert, Jean‐Marie; Watts, Anthony; Pinheiro, Teresa J. T.

doi:10.1046/j.1432-1327.2000.01138.x

Cited by 15 publications

(16 citation statements)

References 29 publications

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“…The secondary structure of the peptide models was also analyzed by FTIR in solid state (pellets) based on the amide I band, which is sensitive to the backbone conformation, and the amide A band associated with intramolecularly hydrogen bonded NH groups 48. The presence of amide I bands at ∼1645 cm −1 provide evidence for the occurrence of α‐helical conformation, for both models, while the higher intensity of amide A band at ∼3300 cm −1 for peptide model 2, compared to peptide model 1, indicates that NHs are strongly hydrogen bonded in agreement with 1 H NMR experiments, MD calculations, and CD spectroscopy.…”

Section: Resultsmentioning

confidence: 99%

Conformational study of new amphipathic α‐helical peptide models of apoA‐I as potential atheroprotective agents

Beaufils¹,

Alexopoulos²,

Petraki³

et al. 2006

Biopolymers

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Aiming at contributing to the development of potential atheroprotective agents, we report on the concept and design of two peptide models, which mimic the amphipathic helices of apoA-I and incorporate Met into their sequences to validate its role as oxidant scavenger: Ac-ESK(Palm)KELSKSW(10)SEM(13)LKEK(Palm)SKS-NH(2) (model 1 [W(10), M(13)]) and Ac-ESK(Palm)KELSKSM(10)SEW(13)LKEK(Palm)SKS-NH(2) (model 2 [M(10), W(13)]). Hydrophobic residues of both models cover about the half of the surface, while the positively and negatively charged residues constitute two separate clusters on the hydrophilic face. Palmitoyl groups were introduced into the Lys-N(epsilon)H(2) groups at positions 3 and 17 to contribute to the amphipathic character of the peptides and stabilize the nonpolar face of the helix. Conformational study by the combined application of 2D-NMR and molecular dynamics simulations, CD, FTIR, and fluorescence spectroscopy revealed that model 1 adopts helical conformation and Met is well exposed to the microenvironment. Model 2 that derives from model 1 by exchanging W(10) (model 1) with M(10) and M(13) (model 1) with W(13) also displays helical characteristics, while Met is rather shielded. Oxidation experiments indicated that model 1 exhibits a 2-fold more potent antioxidant activity towards LDL oxidation, compared to model 2, confirming the role of Met, when is devoid of steric hindrances, as oxidant scavenger for the protection of LDL.

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Section: Resultsmentioning

confidence: 99%

Conformational study of new amphipathic α‐helical peptide models of apoA‐I as potential atheroprotective agents

Beaufils¹,

Alexopoulos²,

Petraki³

et al. 2006

Biopolymers

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“…A summary of the methods used to investigate the structure of immobilized protein layers on gold IS (impedance spectroscopy) [14,32,33], CD [25,34], ATR (attenuated total internal reflectance)-FTIR spectroscopy [35] might be used from the lower side (as opposed to grazing incidence FTIR which must be used from the top and needs a dry sample) but a very thin gold layer is needed. Other methods include AFM [22] and SPR (surface plasmon resonance) [14].…”

Section: Figurementioning

confidence: 99%

Self-assembling layers created by membrane proteins on gold

Shah

Thomas

Phillips

et al. 2007

Biochemical Society Transactions

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Membrane systems are based on several types of organization. First, amphiphilic lipids are able to create monolayer and bilayer structures which may be flat, vesicular or micellar. Into these structures membrane proteins can be inserted which use the membrane to provide signals for lateral and orientational organization. Furthermore, the proteins are the product of highly specific self-assembly otherwise known as folding, which mostly places individual atoms at precise places in three dimensions. These structures all have dimensions in the nanoscale, except for the size of membrane planes which may extend for millimetres in large liposomes or centimetres on planar surfaces such as monolayers at the air/water interface. Membrane systems can be assembled on to surfaces to create supported bilayers and these have uses in biosensors and in electrical measurements using modified ion channels. The supported systems also allow for measurements using spectroscopy, surface plasmon resonance and atomic force microscopy. By combining the roles of lipids and proteins, highly ordered and specific structures can be self-assembled in aqueous solution at the nanoscale.

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“…In the presence of zwitterionic POPC SUV, no effect of membranes on the protein structure could be detected [185]. However, if lysoPhL were taken instead of PhL, a small effect of membranes on the protein structure was observed, leading to the binding and structuring of approximately 60% of the molecules [185,186].…”

Section: Effect Of Different Types Of Phospholipid Membranes On Protementioning

confidence: 98%

“…Collapsing of apoCyt c in the presence of DPPG -SUV was studied by FTIR and H/D exchange [185,186]. In the presence of zwitterionic POPC SUV, no effect of membranes on the protein structure could be detected [185].…”

Section: Effect Of Different Types Of Phospholipid Membranes On Protementioning

confidence: 99%

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How membrane surface affects protein structure

Bychkova

Basova

Balobanov

2014

Biochemistry Moscow

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The immediate environment of the negatively charged membrane surface is characterized by decreased dielectric constant and pH value. These conditions can be modeled by water-alcohol mixtures at moderately low pH. Several globular proteins were investigated under these conditions, and their conformational behavior in the presence of phospholipid membranes was determined, as well as under conditions modeling the immediate environment of the membrane surface. These proteins underwent conformational transitions from the native to a molten globule-like state. Increased flexibility of the protein structure facilitated protein functioning. Our experimental data allow understanding forces that affect the structure of a protein functioning near the membrane surface (in other words, in the membrane field). Similar conformational states are widely reported in the literature. This indicates that the negatively charged membrane surface can serve as a moderately denaturing agent in the cell. We conclude that the effect of the membrane field on the protein structure must be taken into account.

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Structure and dynamics of lipid‐associated states of apocytochrome c

Cited by 15 publications

References 29 publications

Conformational study of new amphipathic α‐helical peptide models of apoA‐I as potential atheroprotective agents

Conformational study of new amphipathic α‐helical peptide models of apoA‐I as potential atheroprotective agents

Self-assembling layers created by membrane proteins on gold

How membrane surface affects protein structure

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