Protein structure, stability and solubility in water and other solvents

Pace, C. Nick; Treviño, Saul; Prabhakaran, Erode N.; Scholtz, J. Martin

doi:10.1098/rstb.2004.1500

Cited by 322 publications

(87 citation statements)

References 82 publications

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“…The harsh organic condition required for PCL ring opening polymerization reaction often presents a challenge for encapsulating sensitive therapeutic biological entities, such as proteins and peptides (Pace, Treviño, Prabhakaran, & Scholtz, 2004;van de Weert, Hennink, & Jiskoot, 2000). The harsh organic condition required for PCL ring opening polymerization reaction often presents a challenge for encapsulating sensitive therapeutic biological entities, such as proteins and peptides (Pace, Treviño, Prabhakaran, & Scholtz, 2004;van de Weert, Hennink, & Jiskoot, 2000).…”

Section: Discussionmentioning

confidence: 99%

“…However, the use of PCL polymer as coating material is not without its drawbacks. The harsh organic condition required for PCL ring opening polymerization reaction often presents a challenge for encapsulating sensitive therapeutic biological entities, such as proteins and peptides (Pace, Treviño, Prabhakaran, & Scholtz, 2004;van de Weert, Hennink, & Jiskoot, 2000). To preserve the functionalities of these biomolecules, extra protection steps (e.g., PEGylation and nanoprecipitation) are required prior to contact with the common organic solvents (Diwan & Park, 2001;Morales-Cruz et al, 2012).…”

Section: Discussionmentioning

confidence: 99%

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Anhydrous polymer‐based coating with sustainable controlled release functionality for facile, efficacious impregnation, and delivery of antimicrobial peptides

Lim

Saravanan

Chong

et al. 2018

Biotech & Bioengineering

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Anhydrous polymers are actively explored as alternative materials to overcome limitations of conventional hydrogel-based antibacterial coating. However, the requirement for strong organic solvent in polymerization reactions often necessitates extra protection steps for encapsulation of target biomolecules, lowering encapsulation efficiency, and increasing process complexity. This study reports a novel coating strategy that allows direct solvation and encapsulation of antimicrobial peptides (HHC36) into anhydrous polycaprolactone (PCL) polymer-based dual layer coating. A thin 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) film is layered onto the peptide-impregnated PCL as a diffusion barrier, to modulate and enhance release kinetics. The impregnated peptides are eventually released in a controlled fashion. The use of 2,2,2-trifluoroethanol (TFE), as polymerization and solvation medium, induces the impregnated peptides to adopt highly stable turned conformation, conserving peptide integrity, and functionality during both encapsulation and subsequent release processes. The dual layer coating showed sustained antibacterial functionality, lasting for 14 days. In vivo assessment using an experimental mouse wounding model demonstrated good biocompatibility and significant antimicrobial efficacy of the coating under physiological conditions. The coating was translated onto silicone urinary catheters and showed promising antibacterial efficacy, even outperforming commercial silver-based Dover cather. This anhydrous polymer-based platform holds immense potential as an effective antibacterial coating to prevent clinical device-associated infections. The simplicity of the coating process enhances its industrial viability.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Anhydrous polymer‐based coating with sustainable controlled release functionality for facile, efficacious impregnation, and delivery of antimicrobial peptides

Lim

Saravanan

Chong

et al. 2018

Biotech & Bioengineering

View full text Add to dashboard Cite

show abstract

“…In contrast, the more general solvophobic effect, which occurs for polar species in an often apolar organic solution and vice versa, has gained much less attention [21][22][23]. This can be mainly explained by the biologically more-relevant investigation of macromolecular conformations in aqueous environments.…”

Section: Introductionmentioning

confidence: 99%

The solvation and ion condensation properties for sulfonated polyelectrolytes in different solvents—a computational study

2014

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In contrast to the broad knowledge about aqueous polyelectrolyte solutions, less is known about the properties in aprotic and apolar solvents. We therefore investigate the behavior of sulfonated polyelectrolytes in sodium form in the presence of different solvents via all-atom molecular dynamics simulations. The results clearly reveal strong variations in ion condensation constants and polyelectrolyte conformations for different solvents like water, dimethyl sulfoxide (DMSO) and chloroform. The binding free energies of the solvent contacts with the polyelectrolyte groups validate the influence of different solvent qualities. With regard to the ion condensation behavior, the numerical findings show that the explicit values for the condensation constants depend on the preferential binding coefficient as derived by the evaluation of Kirkwood-Buff integrals. Surprisingly, the smallest ion condensation constant is observed for DMSO compared to water, whereas in the presence of chloroform, virtually no free ions are present, which is in good agreement to the donor number concept. In contrast to the results for the low condensation constants, the sodium conductivity in DMSO is smaller compared to water. We are able to relate this result to the observed smaller diffusion coefficient for the sodium ions in DMSO.

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“…Protein solubility plays an important role in protein production and application 1–3 . It was estimated that ca.…”

Section: Introductionmentioning

confidence: 99%

Discrimination of soluble and aggregation-prone proteins based on sequence information

Fang

2013

Mol. BioSyst.

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Understanding the factors governing protein solubility is a key to grasp the mechanisms of protein solubility and may provide insight into protein aggregation and misfolding related diseases such as Alzheimer’s disease. In this work, we attempt to identify factors important to protein solubility using feature selection. Firstly, we calculate 1438 features including physicochemical properties and statistics for each protein. Random Forest algorithm is used to select the most informative and the minimal subset of features based on their predictive performance. A predictive model is built based on 17 selected features. Compared with previous models, our model achieves better performance with a sensitivity of 0.82, specificity 0.85, ACC 0.84, AUC 0.91 and MCC 0.67. Furthermore, a model using redundancy-reduced dataset (sequence identity <= 30%) achieves the same performance as the model without redundancy reduction. Our results provide not only a reliable model for predicting protein solubility but also a list of features important to protein solubility. The predictive model is implemented as a freely available web application at http://shark.abl.ku.edu/ProS/.

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Protein structure, stability and solubility in water and other solvents

Cited by 322 publications

References 82 publications

Anhydrous polymer‐based coating with sustainable controlled release functionality for facile, efficacious impregnation, and delivery of antimicrobial peptides

Anhydrous polymer‐based coating with sustainable controlled release functionality for facile, efficacious impregnation, and delivery of antimicrobial peptides

The solvation and ion condensation properties for sulfonated polyelectrolytes in different solvents—a computational study

Discrimination of soluble and aggregation-prone proteins based on sequence information

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