Stabilization of Lysozyme by Benzyl Alcohol: Surface Tension and Thermodynamic Parameters

Goyal, Monu Kumari; Roy, Ipsita; Amin, Aeshna; Banerjee, Uttam Chand; Bansal, Arvind K.

doi:10.1002/jps.22129

Cited by 16 publications

(7 citation statements)

References 50 publications

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“…Two proteins may have similar global stability, but their aggregation pattern can be different because of the differences in the stabilities of their aggregation ‘hot-spots’. In addition, a few exceptions exist in which certain APs were shown to stabilize some proteins 57,58 in contrast to what has been observed in general. It will be interesting to probe the differences between these two types of contradictory behaviors to gain further insight into AP-protein interactions.…”

Section: Discussionmentioning

confidence: 78%

Mechanisms of m-cresol-induced Protein Aggregation Studied Using a Model Protein Cytochrome c

Singh

Hutchings

Mallela

2011

Journal of Pharmaceutical Sciences

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Multi-dose protein formulations require an effective antimicrobial preservative (AP) to inhibit microbial growth during long-term storage of unused formulations. m-cresol is one such AP, but has been shown to cause protein aggregation. However, the fundamental physical mechanisms underlying such AP-induced protein aggregation are not understood. In this study, we used a model protein cytochrome c to identify the protein unfolding that triggers protein aggregation. m-cresol induced cytochrome c aggregation at preservative concentrations that are commonly used to inhibit microbial growth. Addition of m-cresol decreased the temperature at which the protein aggregated and increased the aggregation rate. However, m-cresol did not perturb the tertiary or secondary structure of cytochrome c. Instead, it populated an “invisible” partially unfolded intermediate where a local protein region around the methionine residue at position 80 was unfolded. Stabilizing the Met80 region drastically decreased the protein aggregation, which conclusively shows that this local protein region acts as an aggregation “hot-spot”. Based on these results, we propose that APs induce protein aggregation by partial rather than global unfolding. Because of the availability of site-specific probes to monitor different levels of protein unfolding, cytochrome c provided a unique advantage in characterizing the partial protein unfolding that triggers protein aggregation.

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Section: Discussionmentioning

confidence: 78%

Mechanisms of m-cresol-induced Protein Aggregation Studied Using a Model Protein Cytochrome c

Singh

Hutchings

Mallela

2011

Journal of Pharmaceutical Sciences

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“…Phenolic compounds have been shown to stabilize the R 6 -Zninsulin hexamer (11), which displays the highest physicochemical stability of the commonly manifesting Zn-insulin oligomers (16). Similarly, it has been postulated that benzyl alcohol stabilizes a partially unfolded state of lysozyme due to preferential interactions with that particular conformation, thus inhibiting its further conversion towards more aggregationprone states (17,18). Data from our own group also shows that the addition of excipients which can act as preservatives can increase protein stability, for example by scavenging radicals and thus acting as antioxidants (unpublished results).…”

Section: Introductionmentioning

confidence: 99%

Interactions Between Peptide and Preservatives: Effects on Peptide Self-Interactions and Antimicrobial Efficiency In Aqueous Multi-Dose Formulations

Heljo

Ross

et al. 2015

Pharm Res

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“…As discussed by Yang and Honig 44 and Goyal et al . 45 , a variation of pH can significantly influence the net change on ionisable residues to distress the unfolding free energy. Their studies have demonstrated that for lysozyme the net charge on residues and difference in free energy can be varied around pH 6 and 9.…”

Section: Resultsmentioning

confidence: 99%

Effects of ink characteristics and piezo-electric inkjetting parameters on lysozyme activity

Biswas

Nierstrasz

2019

Sci Rep

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Inkjet printing of enzymes can facilitate many novel applications where a small amount of materials need to be deposited in a precise and flexible manner. However, maintaining the satisfactory activity of inkjet printed enzyme is a challenging task due to the requirements of ink rheology and printhead parameters. Thus to find optimum inkjetting conditions we studied the effects of several ink formulation and jetting parameters on lysozyme activity using a piezoelectric printhead. Within linear activity range of protein concentrations ink containing 50 µg/mL lysozyme showed a satisfactory activity retention of 85%. An acceptable activity of jetted ink was found at pH 6.2 and ionic strength of 0.06 molar. Glycerol was found to be an effective viscosity modifier (10–15 mPa.s), humectant and protein structure stabilizer for the prepared ink. A non-ionic surfactant when used just below critical micelle concentration was found to be favourable for the jetted inks. An increase in activity retention was observed for inks jetted after 24 hours of room temperature incubation. However, no additional activity was seen for inkjetting above the room temperature. Findings of this study would be useful for formulating other protein-based inks and setting their inkjet printing parameters without highly compromising the functionality.

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Stabilization of Lysozyme by Benzyl Alcohol: Surface Tension and Thermodynamic Parameters

Cited by 16 publications

References 50 publications

Mechanisms of m-cresol-induced Protein Aggregation Studied Using a Model Protein Cytochrome c

Mechanisms of m-cresol-induced Protein Aggregation Studied Using a Model Protein Cytochrome c

Interactions Between Peptide and Preservatives: Effects on Peptide Self-Interactions and Antimicrobial Efficiency In Aqueous Multi-Dose Formulations

Effects of ink characteristics and piezo-electric inkjetting parameters on lysozyme activity

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