We recently reported the generation of a highly elastic, crosslinked protein biomaterial via a rapid photochemical process using visible light illumination. In light of these findings, we predicted that other unmodified, tyrosine-rich, self-associating proteins might also be susceptible to this covalent crosslinking method. Here we show that unmodified native fibrinogen can also be photochemically crosslinked into an elastic hydrogel biomaterial through the rapid formation of intermolecular dityrosine. Photochemically crosslinked fibrinogen forms tissue sealant bonds at least 5-fold stronger than commercial fibrin glue and is capable of producing maximum bond strength within 20s. In vitro studies showed that components of the photochemical crosslinking reaction are non-toxic to cells. This material will find useful application in various surgical procedures where rapid curing for high strength tissue sealing is required.
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http://dx.doi.org/10.1016/j.biomaterials.2008.12.059 | DOI Listing |
Biomacromolecules
January 2025
School of Physics and Astronomy, University of Leeds, Leeds LS2 9JT, U.K.
Enzymes are attractive as catalysts due to their specificity and biocompatibility; however, their use in industrial and biomedical applications is limited by stability. Here, we present a facile approach for enzyme immobilization within "all-enzyme" hydrogels by forming photochemical covalent cross-links between the enzyme glucose oxidase. We demonstrate that the mechanical properties of the enzyme hydrogel can be tuned with enzyme concentration and the data suggests that the dimeric nature of glucose oxidase results in unusual gel formation behavior which suggests a degree of forced induced dimer dissociation and unfolding.
View Article and Find Full Text PDFSe Pu
February 2025
CAS Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China.
Chemical modifications are widely used in research fields such as quantitative proteomics and interaction analyses. Chemical-modification targets can be roughly divided into four categories, including those that integrate isotope labels for quantification purposes, probe the structures of proteins through covalent labeling or cross-linking, incorporate labels to improve the ionization or dissociation of characteristic peptides in complex mixtures, and affinity-enrich various poorly abundant protein translational modifications (PTMs). A chemical modification reaction needs to be simple and efficient for use in proteomics analysis, and should be performed without any complicated process for preparing the labeling reagent.
View Article and Find Full Text PDFChemistry
January 2025
Institute of Physiological Chemistry and Pathobiochemistry, University of Münster, Waldeyerstraße 15, 48149, Münster, Germany.
Light-responsive hydrogels are highly valued for their dynamic mechanical properties and biocompatibility. In this study, we present a hydrogel system that can either soften or strengthen on green light exposure, or remain unresponsive to light, depending on the addition of adenosyl cobalamin (AdoCbl) and Co. These protein-based hydrogels were formed using genetically encoded SpyTag-SpyCatcher chemistry and included green light-sensitive CarH protein domains.
View Article and Find Full Text PDFSmall
January 2025
Department of Chemistry, McGill University, 801, Sherbrooke St. West, Montreal, QC, H3A 0B8, Canada.
Oligonucleotide therapeutics, including antisense oligonucleotides and small interfering RNA, offer promising avenues for modulating the expression of disease-associated proteins. However, challenges such as nuclease degradation, poor cellular uptake, and unspecific targeting hinder their application. To overcome these obstacles, spherical nucleic acids have emerged as versatile tools for nucleic acid delivery in biomedical applications.
View Article and Find Full Text PDFAnal Chim Acta
January 2025
State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, School of Material Science and Chemical Engineering, Ningbo University, Ningbo, 315211, PR China. Electronic address:
Background: Foodborne pathogens, particularly Vibrio parahaemolyticus (VP) found in seafood, pose significant health risks, including abdominal pain, nausea, and even death. Rapid, accurate, and sensitive detection of these pathogens is crucial for food safety and public health. However, existing detection methods often require complex sample pretreatment, which limits their practical application.
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