The Experts below are selected from a list of 360 Experts worldwide ranked by ideXlab platform
Kazuhiko Ishihara - One of the best experts on this subject based on the ideXlab platform.
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precise control of surface electrostatic forces on polymer brush layers with opposite charges for resistance to Protein Adsorption
Biomaterials, 2016Co-Authors: Sho Sakata, Yuuki Inoue, Kazuhiko IshiharaAbstract:Various molecular interaction forces are generated during Protein Adsorption process on material surfaces. Thus, it is necessary to control them to suppress Protein Adsorption and the subsequent cell and tissue responses. A series of binary copolymer brush layers were prepared via surface-initiated atom transfer radical polymerization, by mixing the cationic monomer unit and anionic monomer unit randomly in various ratios. Surface characterization revealed that the constructed copolymer brush layers exhibited an uniform super-hydrophilic nature and different surface potentials. The strength of the electrostatic interaction forces operating on these mixed-charge copolymer brush surfaces was evaluated quantitatively using force-versus-distance (f-d) curve measurements by atomic force microscopy (AFM) and probes modified by negatively charged carboxyl groups or positively charged amino groups. The electrostatic interaction forces were determined based on the charge ratios of the copolymer brush layers. Notably, the surface containing equivalent cationic/anionic monomer units hardly interacted with both the charged groups. Furthermore, the Protein Adsorption force and the Protein Adsorption mass on these surfaces were examined by AFM f-d curve measurement and surface plasmon resonance measurement, respectively. To clarify the influence of the electrostatic interaction on the Protein Adsorption behavior on the surface, three kinds of Proteins having negative, positive, and relatively neutral net charges under physiological conditions were used in this study. We quantitatively demonstrated that the amount of adsorbed Proteins on the surfaces would have a strong correlation with the strength of surface-Protein interaction forces, and that the strength of surface-Protein interaction forces would be determined from the combination between the properties of the electrostatic interaction forces on the surfaces and the charge properties of the Proteins. Especially, the copolymer brush surface composed of equivalent cationic/anionic monomer units exhibited no significant interaction forces, and dramatically suppressed the Adsorption of Proteins regardless of their charge properties. We conclude that the established methodology could elucidate relationship between the Protein Adsorption behavior and molecular interaction, especially the electrostatic interaction forces, and demonstrated that the suppression of the electrostatic interactions with the ionic functional groups would be important for the development of new polymeric biomaterials with a high repellency of Protein Adsorption.
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rapid development of hydrophilicity and Protein Adsorption resistance by polymer surfaces bearing phosphorylcholine and naphthalene groups
Langmuir, 2008Co-Authors: Koji Futamura, Madoka Takai, Ryosuke Matsuno, Tomohiro Konno, Kazuhiko IshiharaAbstract:In order to provide a Protein Adsorption resistant surface even when the surface was in contact with a Protein solution under completely dry conditions, a new phospholipid copolymer, poly (2-methacryloyloxyethyl phosphorylcholine (MPC)-co-2-vinylnaphthalene (vN)) (PMvN), was synthesized. Poly(ethylene terephthalate) (PET) could be readily coated with PMvN by a solvent evaporation method. Dynamic contact angle measurements with water revealed that the surface was wetted very rapidly and had strong hydrophilic characteristics; moreover, molecular mobility at the surface was extremely low. When the surface came in contact with a plasma Protein solution containing bovine serum albumin (BSA), the amounts of the plasma Protein adsorbed on the dry surface coated with PMvN and that adsorbed on a dry surface coated with poly(MPC-co-n-butyl methacrylate) (PMB) were compared. Substantially lower Protein Adsorption was observed with PMvN coating. This is due to the rapid hydration behavior of PMvN. We concluded that ...
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rapid development of hydrophilicity and Protein Adsorption resistance by polymer surfaces bearing phosphorylcholine and naphthalene groups
Langmuir, 2008Co-Authors: Koji Futamura, Madoka Takai, Ryosuke Matsuno, Tomohiro Konno, Kazuhiko IshiharaAbstract:In order to provide a Protein Adsorption resistant surface even when the surface was in contact with a Protein solution under completely dry conditions, a new phospholipid copolymer, poly (2-methacryloyloxyethyl phosphorylcholine (MPC)-co-2-vinylnaphthalene (vN)) (PMvN), was synthesized. Poly(ethylene terephthalate) (PET) could be readily coated with PMvN by a solvent evaporation method. Dynamic contact angle measurements with water revealed that the surface was wetted very rapidly and had strong hydrophilic characteristics; moreover, molecular mobility at the surface was extremely low. When the surface came in contact with a plasma Protein solution containing bovine serum albumin (BSA), the amounts of the plasma Protein adsorbed on the dry surface coated with PMvN and that adsorbed on a dry surface coated with poly(MPC-co-n-butyl methacrylate) (PMB) were compared. Substantially lower Protein Adsorption was observed with PMvN coating. This is due to the rapid hydration behavior of PMvN. We concluded that ...
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surface modification on microfluidic devices with 2 methacryloyloxyethyl phosphorylcholine polymers for reducing unfavorable Protein Adsorption
Colloids and Surfaces B: Biointerfaces, 2007Co-Authors: James Sibarani, Madoka Takai, Kazuhiko IshiharaAbstract:Abstract Surface modification of polymer materials for preparing microfluidic devices including poly(dimethyl siloxane) (PDMS) was investigated with phospholipids polymers such as poly(2-methacryloyloxylethyl phosphorylcholine(MPC)-co-n-butyl methacrylate) (PMB) and poly(MPC-co-2-ethylhexyl methacrylate-co-2-(N,N-dimethylamino)ethyl methacrylate) (PMED). The hydrophilicity of every surface on the polymer materials modified with these MPC polymers increased and the value of ζ-potential became close to zero. The Protein Adsorption on the polymer materials with and without the surface modification was evaluated using a Protein mixture of human plasma fibrinogen and serum albumin. Amount of Proteins adsorbed on these polymeric materials showed significant reduction by the surface modification with the MPC polymers compared to the uncoated surfaces ranging from 56 to 90%. Furthermore, we successfully prepared PDMS-based microchannel which was modified by simple coating with the PMB and PMED. The modified microchannel also revealed a significant reduction of Adsorption of serum albumin. We conclude that the MPC polymers are useful for reducing unfavorable Protein Adsorption on microfluidic devices.
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Protein Adsorption from human plasma is reduced on phospholipid polymers
Journal of Biomedical Materials Research, 1991Co-Authors: Kazuhiko Ishihara, Nicholas P Ziats, Brian P Tierney, Nobuo Nakabayashi, James M AndersonAbstract:Protein Adsorption from human plasma was investigated on phospholipid polymers, poly (2-methacryloyloxyethyl phos-phorylcholine (MPC)-co-n-butyl methacrylate (BMA)) or glass by radioim-munoassay and immunogold labeling techniques. In the present studies the focus was to determine the composition and distribution of Proteins at the surface of these materials after contact with human blood plasma. On all materials, Protein Adsorption was detected and included identification of albumin, IgG, fibrinogen, fibronectin, Hageman factor (factor XII), factor VIII/von Willebrand factor, high-molecular-weight kininogen (HMWK) and the complement Protein C5. The amount of Protein adsorbed decreased with an increase in MPC composition and appeared to adsorb to the surfaces in a uniform and evenly distributed manner. Therefore, we suggest that MPC moieties play an important role in suppression of Protein Adsorption. From these findings, it is concluded that the reduction of Protein Adsorption at the blood contacting surface of phospholipid polymers may result in the inhibition of thrombus formation.
Madoka Takai - One of the best experts on this subject based on the ideXlab platform.
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Protein Adsorption behavior on reduced graphene oxide and boron doped diamond investigated by electrochemical impedance spectroscopy
Carbon, 2019Co-Authors: Yixuan Huang, Aiga Hara, Chiaki Terashima, Akira Fujishima, Madoka TakaiAbstract:Abstract As advanced and promising carbon materials, we found reduced graphene oxide (rGO) and boron-doped diamond (BDD) demonstrated special impedance response regarding Protein Adsorption compared with other materials. According to the results of electrochemical impedance spectroscopy (EIS), rGO showed two time constants (two semicircles in Nyquist plot) when exposed to model Protein bovine serum albumin (BSA) solutions; BDD showed decreased impedance response when exposed to high concentration of BSA. They demonstrated special but different impedance response upon BSA Adsorption. Based on fitting results of EIS data and hypothesis of Protein Adsorption, Protein Adsorption model on the interface of Protein solution and carbon electrode surfaces have been established, which is applicable to rGO and BDD surface, and is further expected to be applicable to other carbon materials. Besides the in-depth understanding of Protein Adsorption behavior, this study also indicates a potential way to control the orientations of Protein molecules on solid surface.
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role of interfacial water in Protein Adsorption onto polymer brushes as studied by sfg spectroscopy and qcm
Journal of Physical Chemistry C, 2015Co-Authors: Daiki Nagasawa, Tomoyuki Azuma, Hidenori Noguchi, Kohei Uosaki, Madoka TakaiAbstract:The Adsorption of large biomolecules such as Proteins is of high relevance in medicine; adsorbed Proteins can initiate undesirable biological reactions such as blood coagulation or immune responses, which adversely affect the human body and the functioning of medical devices. Thus, the suppression of Protein Adsorption onto material surfaces is essential for medical and biomedical applications. Interfacial water molecules may play a key role in Protein Adsorption. In this context, in this study, we prepare various types of surfaces (hydrophobic, hydrophilic, anionic, cationic, and zwitterionic) using polymer brushes with different molecular structures. We analyze the Adsorption of negatively and positively charged Proteins using a quartz crystal microbalance (QCM) to quantitatively investigate Protein Adsorption onto the polymer brush surfaces. The structure of the interface between the polymer brushes and water media is investigated using sum frequency generation (SFG) spectroscopy. Our comparison of the...
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rapid development of hydrophilicity and Protein Adsorption resistance by polymer surfaces bearing phosphorylcholine and naphthalene groups
Langmuir, 2008Co-Authors: Koji Futamura, Madoka Takai, Ryosuke Matsuno, Tomohiro Konno, Kazuhiko IshiharaAbstract:In order to provide a Protein Adsorption resistant surface even when the surface was in contact with a Protein solution under completely dry conditions, a new phospholipid copolymer, poly (2-methacryloyloxyethyl phosphorylcholine (MPC)-co-2-vinylnaphthalene (vN)) (PMvN), was synthesized. Poly(ethylene terephthalate) (PET) could be readily coated with PMvN by a solvent evaporation method. Dynamic contact angle measurements with water revealed that the surface was wetted very rapidly and had strong hydrophilic characteristics; moreover, molecular mobility at the surface was extremely low. When the surface came in contact with a plasma Protein solution containing bovine serum albumin (BSA), the amounts of the plasma Protein adsorbed on the dry surface coated with PMvN and that adsorbed on a dry surface coated with poly(MPC-co-n-butyl methacrylate) (PMB) were compared. Substantially lower Protein Adsorption was observed with PMvN coating. This is due to the rapid hydration behavior of PMvN. We concluded that ...
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rapid development of hydrophilicity and Protein Adsorption resistance by polymer surfaces bearing phosphorylcholine and naphthalene groups
Langmuir, 2008Co-Authors: Koji Futamura, Madoka Takai, Ryosuke Matsuno, Tomohiro Konno, Kazuhiko IshiharaAbstract:In order to provide a Protein Adsorption resistant surface even when the surface was in contact with a Protein solution under completely dry conditions, a new phospholipid copolymer, poly (2-methacryloyloxyethyl phosphorylcholine (MPC)-co-2-vinylnaphthalene (vN)) (PMvN), was synthesized. Poly(ethylene terephthalate) (PET) could be readily coated with PMvN by a solvent evaporation method. Dynamic contact angle measurements with water revealed that the surface was wetted very rapidly and had strong hydrophilic characteristics; moreover, molecular mobility at the surface was extremely low. When the surface came in contact with a plasma Protein solution containing bovine serum albumin (BSA), the amounts of the plasma Protein adsorbed on the dry surface coated with PMvN and that adsorbed on a dry surface coated with poly(MPC-co-n-butyl methacrylate) (PMB) were compared. Substantially lower Protein Adsorption was observed with PMvN coating. This is due to the rapid hydration behavior of PMvN. We concluded that ...
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surface modification on microfluidic devices with 2 methacryloyloxyethyl phosphorylcholine polymers for reducing unfavorable Protein Adsorption
Colloids and Surfaces B: Biointerfaces, 2007Co-Authors: James Sibarani, Madoka Takai, Kazuhiko IshiharaAbstract:Abstract Surface modification of polymer materials for preparing microfluidic devices including poly(dimethyl siloxane) (PDMS) was investigated with phospholipids polymers such as poly(2-methacryloyloxylethyl phosphorylcholine(MPC)-co-n-butyl methacrylate) (PMB) and poly(MPC-co-2-ethylhexyl methacrylate-co-2-(N,N-dimethylamino)ethyl methacrylate) (PMED). The hydrophilicity of every surface on the polymer materials modified with these MPC polymers increased and the value of ζ-potential became close to zero. The Protein Adsorption on the polymer materials with and without the surface modification was evaluated using a Protein mixture of human plasma fibrinogen and serum albumin. Amount of Proteins adsorbed on these polymeric materials showed significant reduction by the surface modification with the MPC polymers compared to the uncoated surfaces ranging from 56 to 90%. Furthermore, we successfully prepared PDMS-based microchannel which was modified by simple coating with the PMB and PMED. The modified microchannel also revealed a significant reduction of Adsorption of serum albumin. We conclude that the MPC polymers are useful for reducing unfavorable Protein Adsorption on microfluidic devices.
Shaoyi Jiang - One of the best experts on this subject based on the ideXlab platform.
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pursuing zero Protein Adsorption of poly carboxybetaine from undiluted blood serum and plasma
Langmuir, 2009Co-Authors: Wei Yang, Jinli Zhang, Wei Li, Shaoyi JiangAbstract:Human blood serum and plasma pose significant challenges to blood-contacting devices and implanted materials because of their high nonspecific Adsorption onto surfaces. In this work, we investigated nonspecific Protein Adsorption from single Protein solutions and complex media such as undiluted human blood serum and plasma onto poly(carboxybetaine acrylamide) (polyCBAA)-grafted surfaces at different temperatures. The polyCBAA grafting was done via atom-transfer radical polymerization (ATRP) with varying film thicknesses. The objective is to create a surface that experiences “zero” Protein Adsorption from complex undiluted human blood serum and plasma. Results show that Protein Adsorption from undiluted human blood serum, plasma, and aged serum on the polyCBAA-grafted surface is undetectable at both 25 and 37 °C by a surface plasmon resonance (SPR) sensor. This was achieved with a film thickness of ∼21 nm. Furthermore, it is demonstrated that the polyCBAA surfaces after antibody immobilization maintain und...
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blood compatibility of surfaces with superlow Protein Adsorption
Biomaterials, 2008Co-Authors: Zheng Zhang, Shengfu Chen, Thomas A Horbett, Min Zhang, Buddy D Ratner, Shaoyi JiangAbstract:Abstract In this work, five self-assembled monolayers (SAMs) and three polymeric brushes with very low fibrinogen Adsorption were prepared. The five SAMs are oligo(ethylene glycol) (OEG), phosphorylcholine (PC), oligo(phosphorylcholine) (OPC), and two mixed positively and negatively charged SAMs of SO3−/N+(CH3)3 (SA/TMA) and COO−/N+(CH3)3 (CA/TMA). Three polymer brushes were prepared on gold surfaces via surface-initiated atom transfer radical polymerization (ATRP) using three monomers, sulfobetaine methacrylate (SBMA), carboxybetaine methacrylate (CBMA), and oligo(ethylene glycol) methyl ether methacrylate (OEGMA). Surface plasmon resonance (SPR) measurements show that although all of these surfaces are “nonfouling” to fibrinogen Adsorption from buffer solution, their Protein Adsorption from undiluted human blood plasma varies widely. Polymer brushes exhibit much lower Protein Adsorption from plasma than any of the five SAMs tested. However, platelet adhesion measurements on plasma-preadsorbed surfaces show that all of these surfaces have very low platelet adhesion. Clotting time measurements using recalcified platelet poor plasma (PPP) incubation with the eight types of surfaces show that they do not shorten clotting times. Linear polymers of polySBMA and polyCBMA with similar molecular weights were also synthesized and characterized. In the presence of polyCBMA linear polymers, the clotting time of PPP was prolonged and increased with the concentration of the polymer, while no anticoagulant activity was observed for the polySBMA or PEG polymers. The unique anticoagulant activity of polyCBMA, as well as its high plasma Protein Adsorption resistance, makes polyCBMA a candidate for blood-contacting applications.
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film thickness dependence of Protein Adsorption from blood serum and plasma onto poly sulfobetaine grafted surfaces
Langmuir, 2008Co-Authors: Wei Yang, Shengfu Chen, Jinli Zhang, Gang Cheng, Wei Li, Hana Vaisocherová, Shaoyi JiangAbstract:In this work, we investigate Protein Adsorption from single Protein solutions and complex media such as 100% blood serum and plasma onto poly(sulfobetaine methacrylate) (polySBMA)-grafted surfaces via atom transfer radical polymerization (ATRP) at varying film thicknesses. It is interesting to observe that Protein Adsorption exhibits a minimum at a medium film thickness. Results show that the surface with 62 nm polySBMA brushes presents the best nonfouling character in 100% blood serum and plasma although all of these surfaces are highly resistant to nonspecific Protein Adsorption from single fibrinogen and lysozyme solutions. Surface resistance to 100% blood serum or plasma is necessary for many applications from blood-contacting devices to drug delivery. This work provides a new in vitro evaluation standard for the application of biomaterials in vivo.
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Protein interactions with oligo ethylene glycol oeg self assembled monolayers oeg stability surface packing density and Protein Adsorption
Journal of Biomaterials Science-polymer Edition, 2007Co-Authors: Shengfu Chen, Shaoyi JiangAbstract:We present a study of Protein Adsorption on oligo(ethylene glycol) (OEG) self-assembled monolayers (SAMs) at a range of OEG surface densities. OEG SAMs were formed in mixed ethanol and water solutions at different assembly temperatures to adjust the packing density of EG4-SAMs. These SAMs were characterized using X-ray photoelectron spectroscopy (XPS). Fibrinogen Adsorption on these surfaces was measured by a surface plasmon resonance (SPR) sensor at different temperatures. This work is aimed at addressing three important issues for Protein–OEG interactions, i.e., (i) OEG stability, (ii) the correlation between OEG surface densities and surface non-fouling properties, and (iii) Protein Adsorption on OEG surfaces at different temperatures.
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strong resistance of a thin crystalline layer of balanced charged groups to Protein Adsorption
Langmuir, 2006Co-Authors: Shengfu Chen, Shaoyi JiangAbstract:Resistance of mixed self-assembled monolayers (SAMs) with various counter-charged terminal groups of different valence and protonation/deprotonation states to nonspecific Protein Adsorption is investigated. It is demonstrated that excellent nonfouling surfaces can be readily constructed from mixed positively and negatively charged components of equal valence in a wide range of thiol solution compositions. Furthermore, the lattice structure of one of the mixed SAM systems studied is revealed by atomic force microscopy (AFM) to be (5.2 ± 0.2 A × 5.2 ± 0.2 A)60°. Results indicate that the packing structure of mixed charged SAMs is determined by strong charge−charge interactions of the terminal groups rather than S−Au and chain−chain interactions. This work provides direct evidence that conformational flexibility is not required for Protein resistance of a surface and even a single compact layer of charged groups of balanced charge with a crystalline structure can resist nonspecific Protein Adsorption, sugges...
Feng Chen - One of the best experts on this subject based on the ideXlab platform.
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microwave assisted hydrothermal rapid synthesis of calcium phosphates structural control and application in Protein Adsorption
Nanomaterials, 2015Co-Authors: Zhuyun Cai, Fan Peng, Feng Chen, Qirong QianAbstract:Synthetic calcium phosphate (CaP)-based materials have attracted much attention in the biomedical field. In this study, we have investigated the effect of pH values on CaP nanostructures prepared using a microwave-assisted hydrothermal method. The hierarchical nanosheet-assembled hydroxyapatite (HAP) nanostructure was prepared under weak acidic conditions (pH 5), while the HAP nanorod was prepared under neutral (pH 7) and weak alkali (pH 9) condition. However, when the pH value increases to 11, a mixed product of HAP nanorod and tri-calcium phosphate nanoparticle was obtained. The results indicated that the pH value of the initial reaction solution played an important role in the phase and structure of the CaP. Furthermore, the Protein Adsorption and release performance of the as-prepared CaP nanostructures were investigated by using hemoglobin (Hb) as a model Protein. The sample that was prepared at pH = 11 and consisted of mixed morphologies of nanorods and nanoprisms showed a higher Hb Protein Adsorption capacity than the sample prepared at pH 5, which could be explained by its smaller size and dispersed structure. The results revealed the relatively high Protein Adsorption capacity of the as-prepared CaP nanostructures, which show promise for applications in various biomedical fields such as drug delivery and Protein Adsorption.
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microwave assisted rapid synthesis of magnesium phosphate hydrate nanosheets and their application in drug delivery and Protein Adsorption
Journal of Materials Chemistry B, 2014Co-Authors: Yingjie Zhu, Guanjun Ding, Tuanwei Sun, Feng ChenAbstract:Magnesium phosphate biomaterial, as an alternative to well-known calcium phosphate biomaterials, is an excellent candidate for biomedical applications, owing to its outstanding biocompatibility and biodegradability. Herein, we report a simple strategy for the rapid synthesis of magnesium phosphate hydrate nanosheets (MPHSs) using the microwave-assisted hydrothermal method. This method is facile, rapid, surfactant-free and environmentally friendly. The product shows an excellent ability to promote osteoblast MC-3T3 adhesion and spreading, which indicates high biocompatibility. Moreover, the as-prepared MPHSs are explored for potential applications in the loading and release of the anticancer drug and Protein Adsorption, using docetaxel as a model anticancer drug and hemoglobin (Hb) as a model Protein. The experiments indicate that the as-prepared MPHSs have a relatively high Protein Adsorption capacity and a high ability to damage tumor cells after loading docetaxel. Thus, the as-prepared MPHSs are promising for applications in various biomedical fields such as drug delivery and Protein Adsorption.
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microwave hydrothermal transformation of amorphous calcium carbonate nanospheres and application in Protein Adsorption
ACS Applied Materials & Interfaces, 2014Co-Authors: Yingjie Zhu, Feng ChenAbstract:Calcium carbonate and calcium phosphate are the main components of biominerals. Among all of the forms of biominerals, amorphous calcium carbonate (ACC) and amorphous calcium phosphate (ACP) are the most important forms because they play a pivotal role in the process of biomineralization and are the precursors to the crystalline polymorphs. In this work, we first synthesized ACC in vitro using adenosine 5'-triphosphate disodium salt (ATP) as the stabilizer and investigated the transformation of the ACC under microwave hydrothermal conditions, and ACC/ACP composite nanospheres and carbonated hydroxyapatite (CHA) nanospheres were successfully prepared. In this novel strategy, ATP has two main functions: it serves as the stabilizer for ACC and the phosphorus source for ACP and CHA. Most importantly, the morphology and the size of the ACC precursor can be well-preserved after microwave heating, so it provides a new method for the preparation of calcium phosphate nanostructured materials using phosphorus-containing biomolecule-stabilized ACC as the precursor. Furthermore, the as-prepared ACC/ACP composite nanospheres have excellent biocompatibility and high Protein Adsorption capacity, indicating that they are promising for applications in biomedical fields such as drug delivery and Protein Adsorption.
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hydroxyapatite nanosheet assembled porous hollow microspheres dna templated hydrothermal synthesis drug delivery and Protein Adsorption
Journal of Materials Chemistry, 2012Co-Authors: Chao Qi, Bingqiang Lu, Xinyu Zhao, Jing Zhao, Feng ChenAbstract:Porous hollow microspheres of hydroxyapatite (HAP) are an ideal biomaterial due to their excellent biocompatibility and hollow structure. Herein, we report a novel DNA-templated hydrothermal strategy for the synthesis of HAP nanosheet-assembled hollow microspheres with a nanoporous structure. The as-prepared HAP porous hollow microspheres consist of HAP nanosheets as the building blocks with an average thickness of about 20 nm, and the diameters of the HAP porous hollow microspheres are in the range 2.5–4.5 μm, with an average pore size of about 21.8 nm. The as-prepared HAP porous hollow microspheres are explored for potential applications in drug delivery, and Protein Adsorption and release. The as-prepared HAP porous hollow microspheres show a relatively high drug loading capacity and Protein Adsorption ability, and sustained drug and Protein release, using ibuprofen as a model drug and hemoglobin (Hb) as a model Protein. The experiments indicate that the as-prepared HAP porous hollow microspheres are promising for applications in biomedical fields such as drug delivery and Protein Adsorption.
Frederik R. Wurm - One of the best experts on this subject based on the ideXlab platform.
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Interfacial Conformation of Hydrophilic Polyphosphoesters Affects Blood Protein Adsorption
2018Co-Authors: Christoph Bernhard, Kristin N. Bauer, Mischa Bonn, Frederik R. Wurm, Grazia GonellaAbstract:Synthetic polymers are commonly used as Protein repelling materials for a variety of biomedical applications. Despite their widespread use, the fundamental mechanism underlying Protein repellence is often elusive. Such insights are essential for improving existing and developing new materials. Here, we investigate how subtle differences in the chemistry of hydrophilic polyphosphoesters influence the Adsorption of the human blood Proteins serum albumin and fibrinogen. Using thermodynamic measurements, surface-specific vibrational spectroscopy, and Brewster angle microscopy, we investigate Protein Adsorption, hydration, and steric repulsion properties of the polyphosphoester polymers. Whereas both surface hydration and polymer conformation of the polymers vary substantially as a consequence of the chemical differences in the polymer structure, the Protein repellency ability of these hydrophilic materials appears to be dominated by steric repulsion
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Protein Adsorption is required for stealth effect of poly ethylene glycol and poly phosphoester coated nanocarriers
Nature Nanotechnology, 2016Co-Authors: Susanne Schottle, Greta Ecke, Svenja Winze, Tobias Steinbach, Kristi Moh, Katharina Landfeste, Volke Mailande, Frederik R. WurmAbstract:The current gold standard to reduce non-specific cellular uptake of drug delivery vehicles is by covalent attachment of poly(ethylene glycol) (PEG). It is thought that PEG can reduce Protein Adsorption and thereby confer a stealth effect. Here, we show that polystyrene nanocarriers that have been modified with PEG or poly(ethyl ethylene phosphate) (PEEP) and exposed to plasma Proteins exhibit a low cellular uptake, whereas those not exposed to plasma Proteins show high non-specific uptake. Mass spectrometric analysis revealed that exposed nanocarriers formed a Protein corona that contains an abundance of clusterin Proteins (also known as apolipoProtein J). When the polymer-modified nanocarriers were incubated with clusterin, non-specific cellular uptake could be reduced. Our results show that in addition to reducing Protein Adsorption, PEG, and now PEEPs, can affect the composition of the Protein corona that forms around nanocarriers, and the presence of distinct Proteins is necessary to prevent non-specific cellular uptake.
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Protein Adsorption is required for stealth effect of poly ethylene glycol and poly phosphoester coated nanocarriers
Nature Nanotechnology, 2016Co-Authors: Susanne Schottler, Tobias Steinbach, Greta Becker, Svenja Winzen, Kristin Mohr, Katharina Landfester, Volker Mailander, Frederik R. WurmAbstract:The current gold standard to reduce non-specific cellular uptake of drug delivery vehicles is by covalent attachment of poly(ethylene glycol) (PEG). It is thought that PEG can reduce Protein Adsorption and thereby confer a stealth effect. Here, we show that polystyrene nanocarriers that have been modified with PEG or poly(ethyl ethylene phosphate) (PEEP) and exposed to plasma Proteins exhibit a low cellular uptake, whereas those not exposed to plasma Proteins show high non-specific uptake. Mass spectrometric analysis revealed that exposed nanocarriers formed a Protein corona that contains an abundance of clusterin Proteins (also known as apolipoProtein J). When the polymer-modified nanocarriers were incubated with clusterin, non-specific cellular uptake could be reduced. Our results show that in addition to reducing Protein Adsorption, PEG, and now PEEPs, can affect the composition of the Protein corona that forms around nanocarriers, and the presence of distinct Proteins is necessary to prevent non-specific cellular uptake.
