Isothermal calorimetry: A predictive tool to model drug-propellant interactions in pressurized metered dose systems

Ooi, Jesslynn; Gaisford, Simon; Boyd, Ben J.; Young, Paul M.; Traini, Daniela

doi:10.1016/j.ijpharm.2013.11.055

Cited by 12 publications

(3 citation statements)

References 32 publications

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“…Apparently, the separation of BSA and BLG is more efficient at pH > 7 than at the phase separation pH φ . This is likely due to the much larger binding difference at high pH conditions, which are studied by ITC in Figure and the binding results are listed in Table . − As can be seen from Table , as the pH increases, the binding constant ( K obs ) and binding stoichiometries ( N ) of BLG and BSA both increase, which means a stronger interaction at higher pH. Moreover, the binding affinity difference between BLG and BSA becomes larger at a higher pH, which implies that better selective binding could happen at high pH conditions.…”

Section: Resultsmentioning

confidence: 96%

Selective Protein Separation Based on Charge Anisotropy by Spherical Polyelectrolyte Brushes

et al. 2020

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Protein purification is of vital importance in the food industry, drug discovery, and other related fields. Among many separation methods, polyelectrolyte (PE)-based phase separation was developed and recognized as a low-cost purification technique. In this work, spherical polyelectrolyte brushes (SPBs) with a high specific surface area were utilized to study the protein accessibility and selective protein binding on highly charged nanoparticles (NPs) as well as the selective phase separation of proteins. The correlation between charge anisotropy, protein binding, and phase separation was investigated on various protein systems including those proteins with similar isoelectric points (pI) such as bovine serum albumin (BSA) and β-lactoglobulin (BLG), proteins with similar molecular weights such as BSA and hemoglobin (HB), and even protein variants (BLG-A and -B) with a tiny difference of amino acids. The nonspecific electrostatic interaction studied by turbidimetric titrations and isothermal calorimetry titration (ITC) indicates a specific binding between proteins and SPBs arising from the charge anisotropy of proteins. An optimized output based on selective protein binding on SPBs could be correlated for efficient protein separation through tuning external conditions including pH and ionic strength. These findings, therefore, proved that phase separation based on selective protein adsorption by SPBs was an efficient alternative for protein separation compared with the traditional practice.

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Section: Resultsmentioning

confidence: 96%

Selective Protein Separation Based on Charge Anisotropy by Spherical Polyelectrolyte Brushes

et al. 2020

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“…The isothermal gas perfusion apparatus has been used in a recent study by Ooi et al to investigate the interaction of model propellant 2H,3H-decafluoropentane with beclomethasone dipropionate and salbutamol sulphate [89]. The early stages of beclomethasone dipropionate-decafluoropentane clathrate formation were successfully captured.…”

Section: Gas Perfusion Calorimetrymentioning

confidence: 99%

Determination of physical and chemical stability in pressurised metered dose inhalers: potential new techniques

Ooi

Traini

Boyd

et al. 2015

Expert Opinion on Drug Delivery

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Laser diffraction is well placed to analyse real-time physical stability as a function of particle size; however, its use is restricted to suspension pMDIs. Raman spectroscopy can be potentially used to attain both suspension and solution pMDI spectra in real time; however, the majority of experiments are ex-valve chemical composition mapping. Calorimetry is an effective technique in capturing both chemical and physical degradations of APIs in real time but requires redevelopment to withstand pressure for the purposes of pMDI screening.

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“…It can be used to study solutions, solids and heterogeneous mixtures because it is invariant to sample physical form [8]. This label-free technique is based on heat measurement absorbed or generated during binding event in a sequential (titrating) manner.…”

Section: Introductionmentioning

confidence: 99%

Application of isothermal titration calorimetry in evaluation of protein–nanoparticle interactions

Omanović-Mikličanin

Manfield

Wilkins

2016

J Therm Anal Calorim

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Nanoparticles (NPs) offer a number of advantages over small organic molecules for controlling protein behaviour inside the cell. Protein binding to the surface of NPs depends on their surface characteristics, composition and method of preparation (Mandal et al. in J Hazard Mater 248-249:238-245, 2013). It is important to understand the binding affinities, stoichiometries and thermodynamical parameters of NP-protein interactions in order to see which interaction will have toxic and hazardous consequences and thus to prevent it. On the other side, because proteins are on the brink of stability, they may experience interactions with some types of NPs that are strong enough to cause denaturation or significantly change their conformations with concomitant loss of their biological function. Structural changes in the protein may cause exposure of new antigenic sites, ''cryptic'' peptide epitopes, potentially triggering an immune response which can promote autoimmune disease (Treuel et al. in ACS Nano 8(1):503-513, 2014). Mechanistic details of protein structural changes at NP surface have still remained elusive. Understanding the formation and persistence of the protein corona is critical issue; however, there are no many analytical methods which could provide detailed information about the NP-protein interaction characteristics and about protein structural changes caused by interactions with nanoparticles. The article reviews recent studies in NP-protein interactions research and application of isothermal titration calorimetry (ITC) in this research. The study of protein structural changes upon adsorption on nanoparticle surface and application of ITC in these studies is emphasized. The data illustrate that ITC is a versatile tool for evaluation of interactions between NPs and proteins. When coupled with other analytical methods, it is important analytical tool for monitoring conformational changes in proteins.

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Isothermal calorimetry: A predictive tool to model drug-propellant interactions in pressurized metered dose systems

Cited by 12 publications

References 32 publications

Selective Protein Separation Based on Charge Anisotropy by Spherical Polyelectrolyte Brushes

Selective Protein Separation Based on Charge Anisotropy by Spherical Polyelectrolyte Brushes

Determination of physical and chemical stability in pressurised metered dose inhalers: potential new techniques

Application of isothermal titration calorimetry in evaluation of protein–nanoparticle interactions

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