Probing interactions by means of pulsed field gradient nuclear magnetic resonance spectroscopy

Cozzolino, S.; Sanna, Maria Grazia; Valentini, Massimiliano

doi:10.1002/mrc.2345

Cited by 11 publications

(7 citation statements)

References 61 publications

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“…Like membrane bilayers, micelles provide a hydrophobic-hydrophilic interface, but unlike them, they are small enough to enable solution NMR signals to be observed. Micelles are commonly employed in NMR structure determination of membrane proteins (Qureshi and Goto, 2012;Tulumello and Deber, 2009), but have also been used in studies where the protein-lipid interaction itself is the focus (Cozzolino et al, 2008;Morein et al, 1996;Yu et al, 2006;Romani et al, 2010). NMRbased techniques have been utilized to study an important class of membrane-associated proteins that are called antimicrobial peptides (AMPs).…”

Section: Introductionmentioning

confidence: 99%

Diffusion NMR study of complex formation in membrane-associated peptides

2013

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Pulsed-field-gradient nuclear magnetic resonance (PFG-NMR) is used to obtain the true hydrodynamic size of complexes of peptides with sodium dodecyl sulfate SDS micelles. The peptide used in this study is a 19-residue antimicrobial peptide, GAD-2. Two smaller dipeptides, alanine-glycine (Ala-Gly) and tyrosine-leucine (Tyr-Leu), are used for comparison. We use PFG-NMR to simultaneously measure diffusion coefficients of both peptide and surfactant. These two inputs, as a function of SDS concentration, are then fit to a simple two species model that neglects hydrodynamic interactions between complexes. From this we obtain the fraction of free SDS, and the hydrodynamic size of complexes in a GAD-2-SDS system as a function of SDS concentration. These results are compared to those for smaller dipeptides and for peptide-free solutions. At low SDS concentrations ([SDS] ≤ 25 mM), the results self-consistently point to a GAD-2-SDS complex of fixed hydrodynamic size R = (5.5 ± 0.3) nm. At intermediate SDS concentrations (25 mM < [SDS] < 60 mM), the apparent size of a GAD-2-SDS complex shows almost a factor of two increase without a significant change in surfactant-to-peptide ratio within a complex, most likely implying an increase in the number of peptides in a complex. For peptide-free solutions, the self-diffusion coefficients of SDS with and without buffer are significantly different at low SDS concentrations but merge above [SDS] = 60 mM. We find that in order to obtain unambiguous information about the hydrodynamic size of a peptide-surfactant complex from diffusion measurements, experiments must be carried out at or below [SDS] = 25 mM.

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Section: Introductionmentioning

confidence: 99%

Diffusion NMR study of complex formation in membrane-associated peptides

2013

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“…9 a T 2 cumulative porosity of core sample 1 after the invasion with filter cake (black) and after removing the filter cake (red); b T 2 cumulative porosity of core sample 1 before (red) and after the invasion (black) adapted from (Bageri et al, 2021b) Fig. 10 Relationship between movable water's decrease ratio and permeability damage rate, adapted after (Wu et al 2019(Wu et al ) et al 2007Cozzolino et al 2008;Johns and Gladden 2002). One of the first trail of applying PFG NMR for the sizing of droplets was performed by (Balinov et al 1994) where they investigated the influence of age, water content, and alcohol content on the emulsion droplet size.…”

Section: Emulsion Droplet Size Determination Using Pfg Nmrmentioning

confidence: 99%

A review on the applications of nuclear magnetic resonance (NMR) in the oil and gas industry: laboratory and field-scale measurements

Elsayed

Isah

Hiba

et al. 2022

J Petrol Explor Prod Technol

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This review presents the latest update, applications, techniques of the NMR tools in both laboratory and field scales in the oil and gas upstream industry. The applications of NMR in the laboratory scale were thoroughly reviewed and summarized such as porosity, pores size distribution, permeability, saturations, capillary pressure, and wettability. NMR is an emerging tool to evaluate the improved oil recovery techniques, and it was found to be better than the current techniques used for screening, evaluation, and assessment. For example, NMR can define the recovery of oil/gas from the different pore systems in the rocks compared to other macroscopic techniques that only assess the bulk recovery. This manuscript included different applications for the NMR in enhanced oil recovery research. Also, NMR can be used to evaluate the damage potential of drilling, completion, and production fluids laboratory and field scales. Currently, NMR is used to evaluate the emulsion droplet size and its behavior in the pore space in different applications such as enhanced oil recovery, drilling, completion, etc. NMR tools in the laboratory and field scales can be used to assess the unconventional gas resources and NMR showed a very good potential for exploration and production advancement in unconventional gas fields compared to other tools. Field applications of NMR during exploration and drilling such as logging while drilling, geosteering, etc., were reviewed as well. Finally, the future and potential research directions of NMR tools were introduced which include the application of multi-dimensional NMR and the enhancement of the signal-to-noise ratio of the collected data during the logging while drilling operations.

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“…This complex dependence can be mostly attributed to intermolecular interaction, which is known to be a function of molecular conformation and the potential energy between species [7,11]. Knowledge of intermolecular interactions characterized by structure and energetics is therefore fundamental to a full comprehension of the wide range of protein behaviors.…”

Section: Introductionmentioning

confidence: 99%

Characterization the Effects of Structure and Energetics of Intermolecular Interactions on the Oligomerization of Peptides in Aqueous 2, 2, 2-Trifluoroethanol via Circular Dichroism and Nuclear Magnetic Resonance Spectroscopy

2012

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Intermolecular interactions are of fundamental importance to fully comprehend a wide range of protein behaviors such as oligomerization, folding and recognition. Two peptides, NPY([18-36]) and NPY([15-29]), segmented from human neuropeptide Y (hNPY), were synthesized in this work to study the interaction between species. Information about intermolecular interactions was extracted from their oligomerizing behaviors. The results from CD and NMR showed that the addition of 2, 2, 2-trifluoroethanol (TFE) induces a stable helix in each peptides and an extended helix in NPY([18-36]), formed between residues 30-36. Pulsed field gradient NMR data revealed that NPY([15-29]) forms a larger oligomer at lower temperatures and continuously dissociates into the monomeric form with increasing temperature. NPY([18-36]) was also found to undergo an enhanced interaction with TFE and a more favorable self-association at higher temperatures. We characterized the changes of oligomerized states with respect to temperature to infer the effects of entropy and interaction energy on the association-dissociation equilibrium. As shown by NPY([15-29]), deletion of helical secondary structure or residues from the C-terminal segment may disrupt the solvation by TFE and results in entropy increase as the oligomer dissociates. Unlike that in NPY([15-29]), the extended helix in NPY([18-36]) improves the binding of TFE, and as a result, entropy is gained via the transfer of the TFE cluster from the interface between monomeric peptides into the bulk solvent. This observation suggests that the oligomerized state may be modulated by the entropy and energetics contributed by helical segments in the oligomerization process.

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Probing interactions by means of pulsed field gradient nuclear magnetic resonance spectroscopy

Cited by 11 publications

References 61 publications

Diffusion NMR study of complex formation in membrane-associated peptides

Diffusion NMR study of complex formation in membrane-associated peptides

A review on the applications of nuclear magnetic resonance (NMR) in the oil and gas industry: laboratory and field-scale measurements

Characterization the Effects of Structure and Energetics of Intermolecular Interactions on the Oligomerization of Peptides in Aqueous 2, 2, 2-Trifluoroethanol via Circular Dichroism and Nuclear Magnetic Resonance Spectroscopy

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