Journal articles: 'Protein functionalization'

1

Mateu, M. G. "Virus engineering: functionalization and stabilization." Protein Engineering Design and Selection 24, no. 1-2 (October 5, 2010): 53–63. http://dx.doi.org/10.1093/protein/gzq069.

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Crasson, O., N. Rhazi, O. Jacquin, A. Freichels, C. Jérôme, N. Ruth, M. Galleni, P. Filée, and M. Vandevenne. "Enzymatic functionalization of a nanobody using protein insertion technology." Protein Engineering Design and Selection 28, no. 10 (April 6, 2015): 451–60. http://dx.doi.org/10.1093/protein/gzv020.

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Yoon, Sungkwon, and William T. Nichols. "Nano-functionalization of protein microspheres." Applied Surface Science 309 (August 2014): 106–11. http://dx.doi.org/10.1016/j.apsusc.2014.04.194.

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Wang, Ruidi, Linglan Fu, Junqiu Liu, and Hongbin Li. "Decorating protein hydrogels reversibly enables dynamic presentation and release of functional protein ligands on protein hydrogels." Chemical Communications 55, no. 84 (2019): 12703–6. http://dx.doi.org/10.1039/c9cc06374a.

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Permana, Dani, Herlian Eriska Putra, and Djaenudin Djaenudin. "Designed protein multimerization and polymerization for functionalization of proteins." Biotechnology Letters 44, no. 3 (January 27, 2022): 341–65. http://dx.doi.org/10.1007/s10529-021-03217-8.

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Paolino, Marco, Michela Visintin, Elisa Margotti, Marco Visentini, Laura Salvini, Annalisa Reale, Vincenzo Razzano, et al. "Functionalization of protein hexahistidine tags by functional nanoreactors." New Journal of Chemistry 43, no. 46 (2019): 17946–53. http://dx.doi.org/10.1039/c9nj03463c.

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Meredith, Gavin D., Hayley Y. Wu, and Nancy L. Allbritton. "Targeted Protein Functionalization Using His-Tags." Bioconjugate Chemistry 15, no. 5 (September 2004): 969–82. http://dx.doi.org/10.1021/bc0498929.

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Naskar, Nilanjon, Martin F. Schneidereit, Florian Huber, Sabyasachi Chakrabortty, Lothar Veith, Markus Mezger, Lutz Kirste, et al. "Impact of Surface Chemistry and Doping Concentrations on Biofunctionalization of GaN/Ga‒In‒N Quantum Wells." Sensors 20, no. 15 (July 28, 2020): 4179. http://dx.doi.org/10.3390/s20154179.

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The development of sensitive biosensors, such as gallium nitride (GaN)-based quantum wells, transistors, etc., often makes it necessary to functionalize GaN surfaces with small molecules or even biomolecules, such as proteins. As a first step in surface functionalization, we have investigated silane adsorption, as well as the formation of very thin silane layers. In the next step, the immobilization of the tetrameric protein streptavidin (as well as the attachment of chemically modified iron transport protein ferritin (ferritin-biotin-rhodamine complex)) was realized on these films. The degree of functionalization of the GaN surfaces was determined by fluorescence measurements with fluorescent-labeled proteins; silane film thickness and surface roughness were estimated, and also other surface sensitive techniques were applied. The formation of a monolayer consisting of adsorbed organosilanes was accomplished on Mg-doped GaN surfaces, and also functionalization with proteins was achieved. We found that very high Mg doping reduced the amount of surface functionalized proteins. Most likely, this finding was a consequence of the lower concentration of ionizable Mg atoms in highly Mg-doped layers as a consequence of self-compensation effects. In summary, we could demonstrate the necessity of Mg doping for achieving reasonable bio-functionalization of GaN surfaces.

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De Geyter, Ewout, Eirini Antonatou, Dimitris Kalaitzakis, Sabina Smolen, Abhishek Iyer, Laure Tack, Emiel Ongenae, Georgios Vassilikogiannakis, and Annemieke Madder. "5-Hydroxy-pyrrolone based building blocks as maleimide alternatives for protein bioconjugation and single-site multi-functionalization." Chemical Science 12, no. 14 (2021): 5246–52. http://dx.doi.org/10.1039/d0sc05881e.

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Recent expansion in potential uses of protein conjugates has fueled the development of a range of protein modification methods; however, the desirable single-site multi-functionalization of proteins has remained a particularly intransigent challenge.

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Guzmán-Mendoza, José Jesús, David Chávez-Flores, Silvia Lorena Montes-Fonseca, Carmen González-Horta, Erasmo Orrantia-Borunda, and Blanca Sánchez-Ramírez. "A Novel Method for Carbon Nanotube Functionalization Using Immobilized Candida antarctica Lipase." Nanomaterials 12, no. 9 (April 26, 2022): 1465. http://dx.doi.org/10.3390/nano12091465.

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Carbon nanotubes (CNTs) have been proposed as nanovehicles for drug or antigen delivery since they can be functionalized with different biomolecules. For this purpose, different types of molecules have been chemically bonded to CNTs; however, this method has low efficiency and generates solvent waste. Candida antarctica lipase is an enzyme that, in an organic solvent, can bind a carboxylic to a hydroxyl group by esterase activity. The objective of this work was to functionalize purified CNTs with insulin as a protein model using an immobilized lipase of Candida antarctica to develop a sustainable functionalization method with high protein attachment. The functionalized CNTs were characterized by scanning electron microscope (SEM), Raman spectroscopy, Fourier-transform infrared spectroscopy (FTIR), thermogravimetric analysis (TGA), and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS–PAGE). The enzymatic functionalization of insulin on the surface of the CNTs was found to have an efficiency of 21%, which is higher in conversion and greener than previously reported by the diimide-activated amidation method. These results suggest that enzymatic esterification is a convenient and efficient method for CNT functionalization with proteins. Moreover, this functionalization method can be used to enhance the cellular-specific release of proteins by lysosomal esterases.

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Guzmán-Mendoza, José Jesús, David Chávez-Flores, Silvia Lorena Montes-Fonseca, Carmen González-Horta, Erasmo Orrantia-Borunda, and Blanca Sánchez-Ramírez. "A Novel Method for Carbon Nanotube Functionalization Using Immobilized Candida antarctica Lipase." Nanomaterials 12, no. 9 (April 26, 2022): 1465. http://dx.doi.org/10.3390/nano12091465.

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Carbon nanotubes (CNTs) have been proposed as nanovehicles for drug or antigen delivery since they can be functionalized with different biomolecules. For this purpose, different types of molecules have been chemically bonded to CNTs; however, this method has low efficiency and generates solvent waste. Candida antarctica lipase is an enzyme that, in an organic solvent, can bind a carboxylic to a hydroxyl group by esterase activity. The objective of this work was to functionalize purified CNTs with insulin as a protein model using an immobilized lipase of Candida antarctica to develop a sustainable functionalization method with high protein attachment. The functionalized CNTs were characterized by scanning electron microscope (SEM), Raman spectroscopy, Fourier-transform infrared spectroscopy (FTIR), thermogravimetric analysis (TGA), and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS–PAGE). The enzymatic functionalization of insulin on the surface of the CNTs was found to have an efficiency of 21%, which is higher in conversion and greener than previously reported by the diimide-activated amidation method. These results suggest that enzymatic esterification is a convenient and efficient method for CNT functionalization with proteins. Moreover, this functionalization method can be used to enhance the cellular-specific release of proteins by lysosomal esterases.

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Kim, Min Jung, Guk Hwan An, and Yong Ho Choa. "Functionalization of Magnetite Nanoparticles for Protein Immobilization." Solid State Phenomena 124-126 (June 2007): 895–98. http://dx.doi.org/10.4028/www.scientific.net/ssp.124-126.895.

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The surface of magnetite nanoparticles which have been prepared by coprecipitation method was modified by carboxylic acid group of poly(3-thiophenacetic acid (3TA)). Then the egg white lysozyme was immobilized on the carboxylic acid group of the modification of the magnetite nanoparticles. Lysozyme immobilizing efficiency increased with increasing concentration of 3TA. And the functionalized magnetite particles had higher enzymatic capacity than non-functionalized magnetite nanoparticles.

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KATO, AKIO. "High functionalization of protein by polysaccharide modification." Kagaku To Seibutsu 34, no. 10 (1996): 695–701. http://dx.doi.org/10.1271/kagakutoseibutsu1962.34.695.

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Dinjaski, Nina, and M. Auxiliadora Prieto. "Smart polyhydroxyalkanoate nanobeads by protein based functionalization." Nanomedicine: Nanotechnology, Biology and Medicine 11, no. 4 (May 2015): 885–99. http://dx.doi.org/10.1016/j.nano.2015.01.018.

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Kadam, Reshma, Marina Zilli, Michael Maas, and Kurosch Rezwan. "Nanoscale Janus Particles with Dual Protein Functionalization." Particle & Particle Systems Characterization 35, no. 3 (January 16, 2018): 1700332. http://dx.doi.org/10.1002/ppsc.201700332.

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Zhang, Yuhe, Jiahao Shi, Bin Ma, Ya-Nan Zhou, Haiyang Yong, Jianzhong Li, Xiangyi Kong, and Dezhong Zhou. "Functionalization of polymers for intracellular protein delivery." Progress in Polymer Science 146 (November 2023): 101751. http://dx.doi.org/10.1016/j.progpolymsci.2023.101751.

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Cheng, Quan, Xuan Wang, Xian-En Zhang, Chengchen Xu, and Feng Li. "Quantitative functionalization of biosynthetic caged protein materials." Quantitative Biology 11, no. 1 (2023): 1. http://dx.doi.org/10.15302/j-qb-022-0306.

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Povilonienė, Simona, Vida Časaitė, Virginijus Bukauskas, Arūnas Šetkus, Juozas Staniulis, and Rolandas Meškys. "Functionalization of α-synuclein fibrils." Beilstein Journal of Nanotechnology 6 (January 12, 2015): 124–33. http://dx.doi.org/10.3762/bjnano.6.12.

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The propensity of peptides and proteins to form self-assembled structures has very promising applications in the development of novel nanomaterials. Under certain conditions, amyloid protein α-synuclein forms well-ordered structures – fibrils, which have proven to be valuable building blocks for bionanotechnological approaches. Herein we demonstrate the functionalization of fibrils formed by a mutant α-synuclein that contains an additional cysteine residue. The fibrils have been biotinylated via thiol groups and subsequently joined with neutravidin-conjugated gold nanoparticles. Atomic force microscopy and transmission electron microscopy confirmed the expected structure – nanoladders. The ability of fibrils (and of the additional components) to assemble into such complex structures offers new opportunities for fabricating novel hybrid materials or devices.

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Cagliani, Roberta, Francesca Gatto, and Giuseppe Bardi. "Protein Adsorption: A Feasible Method for Nanoparticle Functionalization?" Materials 12, no. 12 (June 21, 2019): 1991. http://dx.doi.org/10.3390/ma12121991.

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Nanomaterials are now well-established components of many sectors of science and technology. Their sizes, structures, and chemical properties allow for the exploration of a vast range of potential applications and novel approaches in basic research. Biomedical applications, such as drug or gene delivery, often require the release of nanoparticles into the bloodstream, which is populated by blood cells and a plethora of small peptides, proteins, sugars, lipids, and complexes of all these molecules. Generally, in biological fluids, a nanoparticle’s surface is covered by different biomolecules, which regulate the interactions of nanoparticles with tissues and, eventually, their fate. The adsorption of molecules onto the nanomaterial is described as “corona” formation. Every blood particulate component can contribute to the creation of the corona, although small proteins represent the majority of the adsorbed chemical moieties. The precise rules of surface-protein adsorption remain unknown, although the surface charge and topography of the nanoparticle seem to discriminate the different coronas. We will describe examples of adsorption of specific biomolecules onto nanoparticles as one of the methods for natural surface functionalization, and highlight advantages and limitations. Our critical review of these topics may help to design appropriate nanomaterials for specific drug delivery.

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Estupiñán, Diego, Markus B. Bannwarth, Steven E. Mylon, Katharina Landfester, Rafael Muñoz-Espí, and Daniel Crespy. "Multifunctional clickable and protein-repellent magnetic silica nanoparticles." Nanoscale 8, no. 5 (2016): 3019–30. http://dx.doi.org/10.1039/c5nr08258g.

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21

Montroni, Devis, Matteo Di Giosia, Matteo Calvaresi, and Giuseppe Falini. "Supramolecular Binding with Lectins: A New Route for Non-Covalent Functionalization of Polysaccharide Matrices." Molecules 27, no. 17 (September 1, 2022): 5633. http://dx.doi.org/10.3390/molecules27175633.

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The chemical functionalization of polysaccharides to obtain functional materials has been of great interest in the last decades. This traditional synthetic approach has drawbacks, such as changing the crystallinity of the material or altering its morphology or texture. These modifications are crucial when a biogenic matrix is exploited for its hierarchical structure. In this work, the use of lectins and carbohydrate-binding proteins as supramolecular linkers for polysaccharide functionalization is proposed. As proof of concept, a deproteinized squid pen, a hierarchically-organized β-chitin matrix, was functionalized using a dye (FITC) labeled lectin; the lectin used was the wheat germ agglutinin (WGA). It has been observed that the binding of this functionalized protein homogenously introduces a new property (fluorescence) into the β-chitin matrix without altering its crystallographic and hierarchical structure. The supramolecular functionalization of polysaccharides with protein/lectin molecules opens up new routes for the chemical modification of polysaccharides. This novel approach can be of interest in various scientific fields, overcoming the synthetic limits that have hitherto hindered the technological exploitation of polysaccharides-based materials.

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Scheidler, Christopher M., Milan Vrabel, and Sabine Schneider. "Genetic Code Expansion, Protein Expression, and Protein Functionalization in Bacillus subtilis." ACS Synthetic Biology 9, no. 3 (February 13, 2020): 486–93. http://dx.doi.org/10.1021/acssynbio.9b00458.

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Cohn, C., S. L. Leung, J. Crosby, B. Lafuente, Z. Zha, W. Teng, R. Downs, and X. Wu. "Lipid-mediated protein functionalization of electrospun polycaprolactone fibers." Express Polymer Letters 10, no. 5 (2016): 430–37. http://dx.doi.org/10.3144/expresspolymlett.2016.40.

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Fernandes, Margarida M., and Artur Cavaco-Paulo. "Protein disulphide isomerase-assisted functionalization of proteinaceous substrates." Biocatalysis and Biotransformation 30, no. 1 (January 23, 2012): 111–24. http://dx.doi.org/10.3109/10242422.2012.646657.

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Alam, Jenefer, Thomas H. Keller, and Teck-Peng Loh. "Indium mediated allylation in peptide and protein functionalization." Chemical Communications 47, no. 32 (2011): 9066. http://dx.doi.org/10.1039/c1cc12926k.

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Battista, E., P. L. Scognamiglio, G. Das, G. Manzo, F. Causa, E. Di Fabrizio, and P. A. Netti. "Functionalization of Gold-plasmonic Devices for Protein Capture." Procedia Technology 27 (2017): 163–64. http://dx.doi.org/10.1016/j.protcy.2017.04.071.

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Hill, Ryan T., and Jason B. Shear. "Enzyme−Nanoparticle Functionalization of Three-Dimensional Protein Scaffolds." Analytical Chemistry 78, no. 19 (October 2006): 7022–26. http://dx.doi.org/10.1021/ac061102w.

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Borsley, Stefan, and Scott L. Cockroft. "In SituSynthetic Functionalization of a Transmembrane Protein Nanopore." ACS Nano 12, no. 1 (December 19, 2017): 786–94. http://dx.doi.org/10.1021/acsnano.7b08105.

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Chen, Qi, Qing Sun, Nicholas M. Molino, Szu-Wen Wang, Eric T. Boder, and Wilfred Chen. "Sortase A-mediated multi-functionalization of protein nanoparticles." Chemical Communications 51, no. 60 (2015): 12107–10. http://dx.doi.org/10.1039/c5cc03769g.

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A new strategy was developed to create multi-functionalizaton of protein nanoparticles using Sortase A-mediated ligation, resulting in modified protein nanoparticles that are both thermally responsive and catalytic active.

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Wach, Jean-Yves, Barbora Malisova, Simone Bonazzi, Samuele Tosatti, Marcus Textor, Stefan Zürcher, and Karl Gademann. "Protein-Resistant Surfaces through Mild Dopamine Surface Functionalization." Chemistry - A European Journal 14, no. 34 (October 16, 2008): 10579–84. http://dx.doi.org/10.1002/chem.200801134.

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Popescu, Vasilica, Alexandra Cristina Blaga, Melinda Pruneanu, Irina Niculina Cristian, Marius Pîslaru, Andrei Popescu, Vlad Rotaru, Igor Crețescu, and Dan Cașcaval. "Green Chemistry in the Extraction of Natural Dyes from Colored Food Waste, for Dyeing Protein Textile Materials." Polymers 13, no. 22 (November 9, 2021): 3867. http://dx.doi.org/10.3390/polym13223867.

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The beetroot peels can be a sustainable source of betalains that can dye the wool materials through green processes based on low water and energy consumption. Green chemistry in the extraction of betalains from colored food waste/peels from red beetroot involved the use of water as a solvent, without other additives. In order for the extract obtained to be able to dye the wool, it was necessary to functionalize betalains or even the wool. Three types of sustainable functionalizations were performed, with (1) acetic acid; (2) ethanol; and (3) arginine. For each functionalization, the mechanism that can justify dyeing the wool in intense colors was elucidated. The characterization of the extract was performed with the data provided by UV-VIS and HPLC-MS analyses. The characterization of the wool dyed with the extract obtained from the red beetroot peels was possible due to the information resulting from the FTIR and CIELab analyses. The functionalizations of betalains and wool in acid environments lead to the most intense red colors. The color varies depending on the pH and the concentration of betalains.

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Liu, Hai-Jun, and Peisheng Xu. "Smart Mesoporous Silica Nanoparticles for Protein Delivery." Nanomaterials 9, no. 4 (April 2, 2019): 511. http://dx.doi.org/10.3390/nano9040511.

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Mesoporous silica nanoparticles (MSN) have attracted a lot of attention during the past decade which is attributable to their versatile and high loading capacity, easy surface functionalization, excellent biocompatibility, and great physicochemical and thermal stability. In this review, we discuss the factors affecting the loading of protein into MSN and general strategies for targeted delivery and controlled release of proteins with MSN. Additionally, we also give an outlook for the remaining challenges in the clinical translation of protein-loaded MSNs.

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Niemeyer, C. M. "Semi-synthetic DNA–protein conjugates: novel tools in analytics and nanobiotechnology." Biochemical Society Transactions 32, no. 1 (February 1, 2004): 51–53. http://dx.doi.org/10.1042/bst0320051.

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This article reports on the syntheses, characterization and applications of semi-synthetic conjugates composed of nucleic acids, proteins and inorganic nanoparticles. For example, self-assembled oligomeric networks consisting of streptavidin and double-stranded DNA are applicable as reagents in immunoassays, model systems for ion-switchable nanoparticle networks as well as nanometer-scaled ‘soft material’ standards for scanning probe microscopy. Covalent conjugates of single-stranded DNA and streptavidin are utilized as biomolecular adapters for the immobilization of biotinylated macromolecules at solid substrates via nucleic acid hybridization. This ‘DNA-directed immobilization’ allows for reversible and site-selective functionalization of solid substrates with metal and semiconductor nanoparticles or, vice versa, for the DNA-directed functionalization of gold nanoparticles with proteins, such as immunoglobulins and enzymes. This approach is applicable for the detection of chip-immobilized antigens. Moreover, covalent DNA–protein conjugates allow for their selective positioning along single-stranded nucleic acids, and thus for the construction of nanometre-scale assemblies composed of proteins and/or nanoclusters. Examples include the fabrication of functional biometallic nanostructures from gold nanoparticles and antibodies, applicable as diagnostic tools in bioanalytics.

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Huang, Chundong, Da Li, Jun Ren, Fangling Ji, and Lingyun Jia. "Generation and Application of Fluorescent Anti-Human β2-Microglobulin VHHs via Amino Modification." Molecules 24, no. 14 (July 17, 2019): 2600. http://dx.doi.org/10.3390/molecules24142600.

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The functionalization of VHHs enables their application in almost every aspect of biomedical inquiry. Amino modification remains a common strategy for protein functionalization, though is considered to be inferior to site-specific methods and cause protein property changes. In this paper, four anti-β2M VHHs were selected and modified on the amino group by NHS-Fluo. The impacts of amino modification on these VHHs were drastically different, and among all th examples, the modified NB-1 maintained the original stability, bioactivity and homogeneity of unmodified NB-1. Specific recognition of VHHs targeting β2M detected by fluorescence imaging explored the possible applications of VHHs. Via this study, we successfully functionalized the anti-β2M VHHs through amino modification and the results are able to instruct the simple and fast functionalization of VHHs in biomedical researches.

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Gattner, Michael J., Michael Ehrlich, and Milan Vrabel. "Sulfonyl azide-mediated norbornene aziridination for orthogonal peptide and protein labeling." Chem. Commun. 50, no. 83 (2014): 12568–71. http://dx.doi.org/10.1039/c4cc04117h.

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Zacharchenko, Thomas, and Stephanie Wright. "Functionalization of the BCL6 BTB domain into a noncovalent crystallization chaperone." IUCrJ 8, no. 2 (January 11, 2021): 154–60. http://dx.doi.org/10.1107/s2052252520015754.

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The production of diffraction-quality protein crystals is challenging and often requires bespoke, time-consuming and expensive strategies. A system has been developed in which the BCL6 BTB domain acts as a crystallization chaperone and promiscuous assembly block that may form the basis for affinity-capture crystallography. The protein of interest is expressed with a C-terminal tag that interacts with the BTB domain, and co-crystallization leads to its incorporation within a BTB-domain lattice. This strategy was used to solve the structure of the SH3 domain of human nebulin, a structure previously solved by NMR, at 1.56 Å resolution. This approach is simple and effective, requiring only routine protein complexation and crystallization screening, and should be applicable to a range of proteins.

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Ardoino, Niccolò, Lorenzo Lunelli, Georg Pucker, Lia Vanzetti, Rachele Favaretto, Laura Pasquardini, Cecilia Pederzolli, Carlo Guardiani, and Cristina Potrich. "Optimization of Surface Functionalizations for Ring Resonator-Based Biosensors." Sensors 24, no. 10 (May 14, 2024): 3107. http://dx.doi.org/10.3390/s24103107.

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Liquid biopsy is expected to become widespread in the coming years thanks to point of care devices, which can include label-free biosensors. The surface functionalization of biosensors is a crucial aspect that influences their overall performance, resulting in the accurate, sensitive, and specific detection of target molecules. Here, the surface of a microring resonator (MRR)-based biosensor was functionalized for the detection of protein biomarkers. Among the several existing functionalization methods, a strategy based on aptamers and mercaptosilanes was selected as the most highly performing approach. All steps of the functionalization protocol were carefully characterized and optimized to obtain a suitable protocol to be transferred to the final biosensor. The functionalization protocol comprised a preliminary plasma treatment aimed at cleaning and activating the surface for the subsequent silanization step. Different plasma treatments as well as different silanes were tested in order to covalently bind aptamers specific to different biomarker targets, i.e., C-reactive protein, SARS-CoV-2 spike protein, and thrombin. Argon plasma and 1% v/v mercaptosilane were found as the most suitable for obtaining a homogeneous layer apt to aptamer conjugation. The aptamer concentration and time for immobilization were optimized, resulting in 1 µM and 3 h, respectively. A final passivation step based on mercaptohexanol was also implemented. The functionalization protocol was then evaluated for the detection of thrombin with a photonic biosensor based on microring resonators. The preliminary results identified the successful recognition of the correct target as well as some limitations of the developed protocol in real measurement conditions.

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Yan, Sheng, and Yunren Qiu. "Interfacial Interaction between Functionalization of Polysulfone Membrane Materials and Protein Adsorption." Polymers 16, no. 12 (June 10, 2024): 1637. http://dx.doi.org/10.3390/polym16121637.

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This study that modified polysulfone membranes with different end-group chemical functionalities were prepared using chemical synthesis methods and experimentally characterized. The molecular dynamics (MD) method were used to discuss the adsorption mechanism of proteins on functionalized modified polysulfone membrane materials from a molecular perspective, revealing the interactions between different functionalized membrane surfaces and protein adsorption. Theoretical analysis combined with basic experiments and MD simulations were used to explore the orientation and spatial conformational changes of protein adsorption at the molecular level. The results show that BSA exhibits different variability and adsorption characteristics on membranes with different functional group modifications. On hydrophobic membrane surfaces, BSA shows the least stable configuration stability, making it prone to nonspecific structural changes. In addition, surface charge effects lead to electrostatic repulsion for BSA and reduce the protein adsorption sites. These MD simulation results are consistent with experimental findings, providing new design ideas and support for modifying blood-compatible membrane materials.

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Dovgan, Igor, Alexandre Hentz, Oleksandr Koniev, Anthony Ehkirch, Steve Hessmann, Sylvain Ursuegui, Sébastien Delacroix, et al. "Automated linkage of proteins and payloads producing monodisperse conjugates." Chemical Science 11, no. 5 (2020): 1210–15. http://dx.doi.org/10.1039/c9sc05468e.

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Picaud, Fabien, Guillaume Paris, Tijani Gharbi, Sébastien Balme, Mathilde Lepoitevin, Vidhyadevi Tangaraj, Mikhael Bechelany, Jean Marc Janot, Emmanuel Balanzat, and François Henn. "Biomimetic solution against dewetting in a highly hydrophobic nanopore." Soft Matter 12, no. 22 (2016): 4903–11. http://dx.doi.org/10.1039/c6sm00315j.

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Liu, Han, Meihua Yuan, Jegatheeswaran Sonamuthu, Sheng Yan, Wei Huang, Yurong Cai, and Juming Yao. "A dopamine-functionalized aqueous-based silk protein hydrogel bioadhesive for biomedical wound closure." New Journal of Chemistry 44, no. 3 (2020): 884–91. http://dx.doi.org/10.1039/c9nj04545g.

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Falak, Shahkar, Bokyoung Shin, and Dosung Huh. "Modified Breath Figure Methods for the Pore-Selective Functionalization of Honeycomb-Patterned Porous Polymer Films." Nanomaterials 12, no. 7 (March 24, 2022): 1055. http://dx.doi.org/10.3390/nano12071055.

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Recent developments in the field of the breath figure (BF) method have led to renewed interest from researchers in the pore-selective functionalization of honeycomb-patterned (HCP) films. The pore-selective functionalization of the HCP film gives unique properties to the film which can be used for specific applications such as protein recognition, catalysis, selective cell culturing, and drug delivery. There are several comprehensive reviews available for the pore-selective functionalization by the self-assembly process. However, considerable progress in preparation technologies and incorporation of new materials inside the pore surface for exact applications have emerged, thus warranting a review. In this review, we have focused on the pore-selective functionalization of the HCP films by the modified BF method, in which the self-assembly process is accompanied by an interfacial reaction. We review the importance of pore-selective functionalization, its applications, present limitations, and future perspectives.

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Ubeyitogullari, Ali, and Syed S. H. Rizvi. "Heat stability of emulsions using functionalized milk protein concentrate generated by supercritical fluid extrusion." Food & Function 11, no. 12 (2020): 10506–18. http://dx.doi.org/10.1039/d0fo02271c.

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Functionalization of milk protein concentrate by supercritical fluid extrusion enhanced its emulsifying properties, and the resulting emulsions with high protein contents were stable upon heating at 121 °C for 15 min.

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Wijetunge, Anjalee N., Garrett J. Davis, Mehrdad Shadmehr, Julia A. Townsend, Michael T. Marty, and John C. Jewett. "Copper-Free Click Enabled Triazabutadiene for Bioorthogonal Protein Functionalization." Bioconjugate Chemistry 32, no. 2 (January 25, 2021): 254–58. http://dx.doi.org/10.1021/acs.bioconjchem.0c00677.

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Sebeika, Meaghan M., Nicholas G. Gedeon, Sara Sadler, Nicholas L. Kern, Devan J. Wilkins, David E. Bell, and Graham B. Jones. "Protein and antibody functionalization using continuous flow microreactor technology." Journal of Flow Chemistry 5, no. 3 (September 2015): 151–54. http://dx.doi.org/10.1556/1846.2015.00008.

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Weng, Yejing, Bo Jiang, Kaiguang Yang, Zhigang Sui, Lihua Zhang, and Yukui Zhang. "Polyethyleneimine-modified graphene oxide nanocomposites for effective protein functionalization." Nanoscale 7, no. 34 (2015): 14284–91. http://dx.doi.org/10.1039/c5nr03370e.

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Schoonen, Lise, and Jan C. M. van Hest. "Functionalization of protein-based nanocages for drug delivery applications." Nanoscale 6, no. 13 (2014): 7124–41. http://dx.doi.org/10.1039/c4nr00915k.

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Asano, Ryutaro, and Izumi Kumagai. "Functionalization of Bispecific Therapeutic Antibodies Based on Protein Engineering." YAKUGAKU ZASSHI 135, no. 7 (July 1, 2015): 851–56. http://dx.doi.org/10.1248/yakushi.15-00007-2.

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Arroyo-Hernández, María, Rafael Daza, Jose Pérez-Rigueiro, Manuel Elices, Jorge Nieto-Márquez, and Gustavo V. Guinea. "Optimization of functionalization conditions for protein analysis by AFM." Applied Surface Science 317 (October 2014): 462–68. http://dx.doi.org/10.1016/j.apsusc.2014.07.201.

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Carneiro, Lara A. B. C., and Richard J. Ward. "Functionalization of paramagnetic nanoparticles for protein immobilization and purification." Analytical Biochemistry 540-541 (January 2018): 45–51. http://dx.doi.org/10.1016/j.ab.2017.11.005.

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Journal articles on the topic 'Protein functionalization'

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