New hydrogel based on polyethylene glycol cross-linked with bovine serum albumin

D'Urso, Edith Marie; Fortier, Guy

doi:10.1007/bf00152843

Cited by 18 publications

(9 citation statements)

References 8 publications

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“…23,24 While the primary structure of albumin contains as much as 59 lysine residues, 25 altogether, 25−35 of them can be targeted for PTM-related reactions in vitro. 10,26,27 Through the versatility of its PTMs, albumin has become a model protein for many applications ranging from the construction of such polymer−protein conjugates in materials science, nanomedicine, and polymer chemistry 8 to, for example, initial spinlabeling studies in EPR spectroscopy. 28−30 Recent progress in controlled radical polymerization techniques, including atom transfer radical polymerization (ATRP), 31 has triggered increased interest in the development of protein macroinitiators that provide access to polymer− protein conjugates in a "grafting-from" approach.…”

Section: ■ Introductionmentioning

confidence: 99%

“…As major transport proteins in blood plasma, albumins are subjected to a broad variety of subtle physiological PTMs as, for example, glycosylation, , acetylation, , noncovalent uptake of cofactors, ligands and ions, , modification of the redox-active Cys34 residue, − and the highly reactive lysine residues. , While the primary structure of albumin contains as much as 59 lysine residues, altogether, 25–35 of them can be targeted for PTM-related reactions in vitro. ,, Through the versatility of its PTMs, albumin has become a model protein for many applications ranging from the construction of such polymer–protein conjugates in materials science, nanomedicine, and polymer chemistry to, for example, initial spin-labeling studies in EPR spectroscopy. − …”

Section: Introductionmentioning

confidence: 99%

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Ligand-Binding Cooperativity Effects in Polymer–Protein Conjugation

et al. 2019

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We present an electron paramagnetic resonance (EPR) spectroscopic characterization of structural and dynamic effects that stem from post-translational modifications of bovine serum albumin (BSA), an established model system for polymer–protein conjugation. Beyond the typical drug delivery and biocompatibility aspect of such systems, we illustrate the causes that alter internal dynamics and therefore functionality in terms of ligand-binding to the BSA protein core. Uptake of the paramagnetic fatty acid derivative 16-doxyl stearic acid by several BSA-based squaric acid macroinitiators and polymer–protein conjugates was studied by EPR spectroscopy, aided by dynamic light scattering (DLS) and zeta potential measurements. The conjugates were grafted from oligo(ethylene glycol) methyl ether methacrylate (OEGMA), forming an overall core–shell-like structure. It is found that ligand-binding and associated parameters such as binding affinity, cooperativity, and the number of binding sites of BSA change drastically with the extent of surface modification. In the course of processing BSA, the ligands also change their preference for individual binding sites, as observed from a comparative view of their spatial alignments in double electron electron resonance (DEER) experiments. The protein-attached polymers constitute a diffusion barrier that significantly hamper ligand uptake. Moreover, zeta potentials (ζ) decrease linearly with the degree of surface modification in protein macroinitiators and an effective dielectric constant can be estimated for the polymer layer in the conjugates. All this suggests that ligand uptake characteristics in BSA can be fine-tuned by the extent and nature of such post-translational modifications (PTMs). We show that EPR spectroscopy is suitable for quantifying these subtle PTM-based functional effects from self-assembly of substrate and ligand.

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Section: ■ Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Ligand-Binding Cooperativity Effects in Polymer–Protein Conjugation

et al. 2019

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“…New bioartificial polymeric materials which combine properties of synthetic and natural polymers may overcome the deficiencies of synthetic polymers and enhance the mechanical properties of biopolymers, leading to a better composite material (3). In agreement with this point of view, we have recendy introduced a new family of bioartificial hydrogels prepared by cross-linking activated poly(ethylene glycol) (PEG) of various molecular masses with bovine serum albumin (BSA) (4). We present herein the characterization and some physical properties of a hydrogel made with PEG of molecular mass of 8000 (BSA-PEG 8000).…”

mentioning

confidence: 65%

New Bioartificial Hydrogels: Characterization and Physical Properties

Gayet

Fortier

1996

ACS Symposium Series

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Physical properties of a bioartificial hydrogel prepared by cross-linking activated poly(ethylene glycol) of molecular mass of 8000 with bovine serum albumin (BSA) are described. This hydrogel shows a great swelling capacity and a high equilibrium water content (EWC > 95%). The volume expansion factor of a BSA-PEG 8000 hydrogel during swelling was a function of its initial thickness. This hydrogel shows a high elasticity since it was reversibly deformable until a level of compression of 60% and it broke only when this level reached 80%. DSC heating scans demonstrated that differentiation of two kinds of water in the hydrogel is possible : the free (bulk) and the bound water. There was evidence that bound water is in the form of a trihydrate complex with ethylene oxide units of the PEG in the network. This hydrogel was suitable for controlled drug release systems, as demonstrated with release experiments.Hydrogels have attracted significant attention during the last decade for their potential use in the biomedical field (1-2). They are a hydrophilic polymeric network which is glassy in the dehydrated state and which swells in the presence of water to form an elastic gel. Whether they are of natural or synthetic origin, they share a high water content, a permeability to small (even large) molecules, a cross-linked structure and a potentially good biocompatibility. Biomedical applications of hydrogels are extending into areas such as materials for blood contact, contact lenses, artificial tendons, controlled release devices, bioadhesive materials, and so forth. Since synthetic polymers are available with a wide variety of compositions, properties and forms, and exhibit good mechanical behaviour, they often lack biocompatibility in living systems, whereas natural polymers have the opposite properties. New bioartificial polymeric materials which combine properties of synthetic and natural polymers may overcome the deficiencies of synthetic polymers and enhance the mechanical properties of biopolymers, leading to a better composite material (3). In agreement with this point of view, we have recendy introduced a new family of bioartificial hydrogels prepared by cross-linking activated poly(ethylene glycol) (PEG) of various molecular masses with bovine serum albumin (BSA) (4). We present herein the characterization and some physical properties of a hydrogel made with PEG of molecular mass of 8000 (BSA-PEG 8000).

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“…Numerous reports on this method can be found in the literature. For example ribonuclease,3 superoxide dismutase,3, 4 horseradish peroxidase,4 lipase,6, 7 and bovine serum albumin8 were modified by monomethoxy‐polyethylene glycol derivatives. Lipase was also modified by various other synthetic polymers 9…”

Section: Introductionmentioning

confidence: 99%

Immobilization of ?-chymotrypsin for use in batch and continuous reactors

Mohapatra

Hsu

2000

J. Chem. Technol. Biotechnol.

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a-Chymotrypsin from bovine pancrease (EC 3.4.21.1) was entrapped in Ca-alginate gel particles to carry out hydrolysis of N-acetyl-L-phenylalanine methyl ester (APME) in batch as well as continuous ®xed bed reactor. The enzyme was covalently modi®ed with homo-bifunctional polyethylene glycol derivatives in order to reduce its leakage from the beads; 85% modi®cation of the P-NH 2 groups of lysine residues caused reduction in the enzyme activity by 50%. However, this modi®cation was helpful in a long run because it reduced both enzyme leakage and deactivation. Effective diffusivities and the distribution coef®cients of the substrate and the product were determined experimentally, and later used in simulation of a batch experiment employing the beads. A continuous ®xed bed reactor with the gel beads was operated to study the deactivation of the enzyme. During a 15-day period, the enzyme showed about 15% loss in the conversion which occurred only during the ®rst 5 days. After that the enzyme did not deactivate further which demonstrates that this method can be applied for continuous reactions.

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New hydrogel based on polyethylene glycol cross-linked with bovine serum albumin

Cited by 18 publications

References 8 publications

Ligand-Binding Cooperativity Effects in Polymer–Protein Conjugation

Ligand-Binding Cooperativity Effects in Polymer–Protein Conjugation

New Bioartificial Hydrogels: Characterization and Physical Properties

Immobilization of ?-chymotrypsin for use in batch and continuous reactors

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