Micro‐ and macro‐phase behavior in protein‐polyelectrolyte complexes

Mattison, Kevin; Wang, Yingfan; Grymonpré, Kris; Dubin, Paul L.

doi:10.1002/masy.19991400107

Cited by 38 publications

(46 citation statements)

References 19 publications

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“…Values of pH at which there are solubilization or biopolymer complexes formation do not depend or depend very little on the total concentration of the biopolymers. On the other hand, they are strongly related to the isoelectric point of the protein, the ratio between the biopolymers, their ionic strength and molar mass [10][11][12] . Given this context, the aim of this study was to characterize the soy protein isolate and high-methoxyl pectin biopolymers through solubility, charges, turbidimetry, and optical microscopy analyses, besides characterizing the complex formed by the pair at different proportions and pHs, evaluating turbidimetry and optical microscopy.…”

Section: Introductionmentioning

confidence: 99%

Characterization of biopolymers and soy protein isolate-high-methoxyl pectin complex

2017

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ObstractThis study aimed at characterizing the soy protein isolate and high-methoxyl pectin biopolymers individually, and the complexes formed by both at different proportions and pHs in order to find the most suitable pH and biopolymer ratios to food application as stabilizers. The biopolymers were evaluated through solubility, charges, turbidimetry, and optical microscopy analyses; the systems with the pair of biopolymers were analyzed through turbidimetry and optical microscopy. High-methoxyl pectin showed high solubility at all pHs investigated. The soy protein isolate showed low solubility at pH 4.5, which is close to its isoelectric point, and complete solubility at pH 11.0. The formation of complexes suggested an attractive interaction between the biopolymers, with high absorbance reading values and images of complexes from optical microscopy. These complexes were present in systems with pHs below the soy protein isolate's isoelectric point, with positive charges; the high-methoxyl pectin, however, had negative ones.

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Section: Introductionmentioning

confidence: 99%

Characterization of biopolymers and soy protein isolate-high-methoxyl pectin complex

2017

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“…Indeed, a theoretical study indicated that proteins form electrostatically stabilised complexes with polyelectrolytes and that the formation of these complexes is mainly regulated by the surface charge of the proteins [51]. Experimental work proved that complex formation between a polyelectrolyte and a protein may take place even close to the isoelectric point (pI) of the protein where the net charge is essentially zero but regional charged patches would still exist [52,53]. In a separate study it was found that positively charged therapeutic antibodies bound to homogenised rat SC tissue in a way that was dependent of both pH and the ionic strength, indicating that electrostatic interactions were playing a role in determining the extent of absorption of these antibodies from the SC injection site [54].…”

Section: Electrostatic Interactionsmentioning

confidence: 99%

Improving the outcomes of biopharmaceutical delivery via the subcutaneous route by understanding the chemical, physical and physiological properties of the subcutaneous injection site

Kinnunen

Mrsny

2014

Journal of Controlled Release

135

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Publisher's copyright statement: NOTICE: this is the author's version of a work that was accepted for publication in Journal of Controlled Release. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reected in this document. Changes may have been made to this work since it was submitted for publication. A denitive version was subsequently published in Journal of Controlled Release, 182, 2014Release, 182, , 10.1016Release, 182, /j.jconrel.2014.011. Additional information:Use policyThe full-text may be used and/or reproduced, and given to third parties in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-prot purposes provided that:• a full bibliographic reference is made to the original source • a link is made to the metadata record in DRO • the full-text is not changed in any way The full-text must not be sold in any format or medium without the formal permission of the copyright holders.Please consult the full DRO policy for further details. AbstractSubcutaneous (SC) injection is currently the most common route of self-administering biopharmaceuticals such as proteins and peptides. While pharmaceutical scientists have acquired great skill in identifying formulations for these as proteins and peptides with multi-year shelf life stability, the SC injection of these formulations can result in inconsistent or particularly low bioavailability outcomes. We hypothesise that upon injection, the chemical, physical and physiological properties of the subcutaneous tissue may play a crucial role in determining the therapeutic outcomes of SC injected biopharmaceuticals. We contend that physical and chemical stresses placed upon the injected protein or peptide as is transitions from the non-physiological environment of its formulation to the homeostatic conditions of the SC tissue can affect its fate following injection. In this mini-review we describe how events that occur to an injected protein or peptide during this post-injection transition period could affect the diffusion of bioactive material to blood capillaries and lymphatic vessels. With this in mind, we have reviewed the chemical, physical and physiological attributes of the SC tissue and collated studies on how these properties are known to affect protein stability and diffusional properties. Finally, examples where the understanding of the properties of the SC tissue when formulating for SC injected biopharmaceuticals has improved the predictability of drug delivery via the SC route are discussed, with the need for novel tools for rational and informed formulation development is highlighted.

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“…The most critical parameter is the solution pH, relatively to the protein isoelectric point (IP). Coulombic interactions between a protein and a polyelectrolyte lead to phase separation through the formation of protein/polyelectrolyte complexes at pH lower than IP with polyanions and at pH higher than IP with polycations [4][5][6][7][8]. Such protein/polyelectrolyte complexes play a major role in many processes, biological and chemical, like drug delivery [9,10], and protein separation [4,11,12].…”

Section: Introductionmentioning

confidence: 99%

“…Coulombic interactions between a protein and a polyelectrolyte lead to phase separation through the formation of protein/polyelectrolyte complexes at pH lower than IP with polyanions and at pH higher than IP with polycations [4][5][6][7][8]. Such protein/polyelectrolyte complexes play a major role in many processes, biological and chemical, like drug delivery [9,10], and protein separation [4,11,12]. Many studies have been focused in a wide range of pH and in various ionic strengths [13][14][15], examining the complex coacervation [7,11,13,16], as well as the size and mobility of the complexes formed [4,15,17].…”

Section: Introductionmentioning

confidence: 99%

“…Such protein/polyelectrolyte complexes play a major role in many processes, biological and chemical, like drug delivery [9,10], and protein separation [4,11,12]. Many studies have been focused in a wide range of pH and in various ionic strengths [13][14][15], examining the complex coacervation [7,11,13,16], as well as the size and mobility of the complexes formed [4,15,17]. Turbidimetry [4], static and dynamic light scattering [5], potentiometry [6], electrophoresis [17], fluorescence [18], and other techniques have been used to provide information about protein/polyelectrolyte complexes.…”

Section: Introductionmentioning

confidence: 99%

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Complexation of bovine serum albumin with cationic polyelectrolytes at pH 7.40 – Formation of soluble complexes

Asimakopoulos

Staikos

2015

European Polymer Journal

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Micro‐ and macro‐phase behavior in protein‐polyelectrolyte complexes

Cited by 38 publications

References 19 publications

Characterization of biopolymers and soy protein isolate-high-methoxyl pectin complex

Characterization of biopolymers and soy protein isolate-high-methoxyl pectin complex

Improving the outcomes of biopharmaceutical delivery via the subcutaneous route by understanding the chemical, physical and physiological properties of the subcutaneous injection site

Complexation of bovine serum albumin with cationic polyelectrolytes at pH 7.40 – Formation of soluble complexes

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