Analysis of the pH-dependent stability and millisecond folding kinetics of horse cytochrome c

Jain, Rishu; Kumar, Rajesh; Kumar, Sandeep; Chhabra, Ritika; Agarwal, Mukesh Chand

doi:10.1016/j.abb.2015.09.011

Cited by 14 publications

(11 citation statements)

References 116 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…At the same time, the solution's pH decreased, and the surface charge of the amphiphilic protein was accordingly tuned to positive. 53 As is shown in Fig. 6, this resulted in low interest, or even repulsion, between the acidic cytochrome c and the protonated hydrogels, which corresponded to the NIP hydrogels in 10-50 mM HCl and MIP hydrogels in 30-50 mM HCl.…”

Section: Specificitymentioning

confidence: 80%

Specific recognition of a target protein, cytochrome c, using molecularly imprinted hydrogels

2022

View full text Add to dashboard Cite

show abstract

Section: Specificitymentioning

confidence: 80%

Specific recognition of a target protein, cytochrome c, using molecularly imprinted hydrogels

2022

View full text Add to dashboard Cite

show abstract

“…The complex is precipitated at concentrations above 30 µmol·L −1 (at pH 7.4). At pH 5.5, molecular solubility drops down significantly ( Table 1 ) due to a change in the unfolding properties of ferricytochrome c and a decrease in its stability with acidity [ 34 ]. In thermal lens experiments with freshly prepared ferricytochrome c solutions, this effect seems to be absent, although a significant drop in the thermal lens signal for low pHs is found after several hours ( Figure 5 ); the signal for pH 7.4 changes insignificantly, although the complex compositions found for lower signals, differed insignificantly.…”

Section: Discussionmentioning

confidence: 99%

Composition of the Cytochrome c Complex with Cardiolipin by Thermal Lens Spectrometry

et al. 2023

View full text Add to dashboard Cite

Thermal lens spectrometry along with spectrophotometric titration were used to assess the composition of the complex of oxidized cytochrome c (ferricytochrome c) with 1,1′,2,2′-tetraoleyl cardiolipin, which plays a key role in the initiation of apoptosis. Spectrophotometric titration was carried out for micromolar concentrations at which the complex is mainly insoluble, to assess the residual concentration in the solution and to estimate the solubility of the complex. Thermal lens spectrometry was used as a method of molecular absorption spectroscopy, which has two advantages over conventional optical transmission spectroscopy: the higher sensitivity of absorbance measurements and the possibility of studying the light absorption by chromophores and heat transfer in complex systems, such as living cells or tissues. Thermal lens measurements were carried out at nanomolar concentrations, where the complex is mainly in solution, i.e., under the conditions of its direct measurements. From the thermal lens measurements, the ratios of cytochrome c and cardiolipin in the complex were 50 at pH 7.4; 30 at pH 6.8; and 10 at pH 5.5, which fit well to the spectrophotometric data. The molecular solubility of the complex at pH 6.8–7.4 was estimated as 30 µmol/L.

show abstract

“…Low pH treatments are commonly used in therapeutic protein manufacturing to inactivate enveloped viruses through lipid hydrolysis and protein structural changes . Values of pH between 3.4 and 4.2 can fully inactivate enveloped viruses given the ideal time frame for the specific virus .…”

Section: Traditional Enveloped Virus Inactivationmentioning

confidence: 99%

Arginine‐enveloped virus inactivation and potential mechanisms

Meingast

Heldt

2019

Biotechnology Progress

View full text Add to dashboard Cite

Arginine synergistically inactivates enveloped viruses at a pH or temperature that does little harm to proteins, making it a desired process for therapeutic protein manufacturing. However, the mechanisms and optimal conditions for inactivation are not fully understood, and therefore, arginine viral inactivation is not used industrially. Optimal solution conditions for arginine viral inactivation found in the literature are high arginine concentrations (0.7–1 M), a time of 60 min, and a synergistic factor of high temperature (≥40°C), low pH (≤pH 4), or Tris buffer (5 mM). However, at optimal conditions full inactivation does not occur over all enveloped viruses. Enveloped viruses that are resistant to arginine often have increased protein stability or membrane stabilizing matrix proteins. Since arginine can interact with both proteins and lipids, interaction with either entity may be key to understanding the inactivation mechanism. Here, we propose three hypotheses for the mechanisms of arginine induced inactivation. Hypothesis 1 describes arginine‐induced viral inactivation through inhibition of vital protein function. Hypothesis 2 describes how arginine destabilizes the viral membrane. Hypothesis 3 describes arginine forming pores in the virus membrane, accompanied by further viral damage from the synergistic factor. Once the mechanisms of arginine viral inactivation are understood, further enhancement by the addition of functional groups, charges, or additives may allow the inactivation of all enveloped viruses in mild conditions.

show abstract

Analysis of the pH-dependent stability and millisecond folding kinetics of horse cytochrome c

Cited by 14 publications

References 116 publications

Specific recognition of a target protein, cytochrome c, using molecularly imprinted hydrogels

Specific recognition of a target protein, cytochrome c, using molecularly imprinted hydrogels

Composition of the Cytochrome c Complex with Cardiolipin by Thermal Lens Spectrometry

Arginine‐enveloped virus inactivation and potential mechanisms

Contact Info

Product

Resources

About