A protein-engineered triblock copolymer hydrogel composed of two self-assembling domains (SADs) has been fabricated by a photoactivatable diazirine group followed by ultraviolet (UV)-mediated crosslinking. The photocrosslinkable protein polymer CEC-D has been patterned into various features including different micrometer-scale stripes by using lithographic techniques. The patterned hydrogels are important for encapsulation of small molecules where a photopatterned fraction of 50% is optimal for maximum absorption. Stripe-patterned CEC-D exhibits slightly lower swelling ratios, an 8.9 times lower erosion profile, and a 2.6-fold higher drug release compared to the unpatterned hydrogel control, CEC-D. Our studies demonstrate the potential of photocrosslinkable protein polymer hydrogels to be used as scaffolds for therapeutic delivery of small molecules. Through photolithographic techniques on the protein hydrogel, a variety of functionalities can be achieved by patterning different features enabling the mimicry of biological systems.
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http://dx.doi.org/10.1021/acs.biomac.0c00616 | DOI Listing |
The 26S proteasome complex is the hub for regulated protein degradation in the cell. It is composed of two biochemically distinct complexes: the 20S core particle with proteolytic active sites in an internal chamber and the 19S regulatory particle, consisting of a lid and base subcomplex. The base contains ubiquitin receptors and an AAA+ (ATPases associated with various cellular activities) motor that unfolds substrates prior to degradation.
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December 2024
Laboratory of Neurochemical Biology, Peking-Tsinghua Center for Life Sciences, Peking-Tsinghua-NIBS (PTN) Graduate Program, School of Life Sciences, Peking University, Beijing, China; Chinese Institute for Brain Research (CIBR), Beijing, China; Department of Chemical Biology, College of Chemistry and Chemical Engineering; School of Pharmaceutical Sciences, PKU-IDG/McGovern Institute for Brain Research, Peking University, Beijing, China; Chinese Institutes for Medical Research (CIMR), Beijing, China; Capital Medical University, Beijing, China. Electronic address:
Research into mechanisms underlying sleep traditionally relies on electrophysiology and genetics. Because sleep can only be measured on whole animals by behavioral observations and physical means, no sleep research was initiated by biochemical and chemical biological approaches. We used phosphorylation sites of kinases important for sleep as targets for biochemical and chemical biological approaches.
View Article and Find Full Text PDFACS Chem Biol
December 2024
Biomedical Science Research Complex, Schools of Biology and Chemistry, University of Saint Andrews, North Haugh, St Andrews KY16 9ST, United Kingdom of Great Britain and Northern Ireland.
Click chemistry is an immensely powerful technique for the synthesis of reliable and efficient covalent linkages. When undertaken in living cells, the concept is thereby coined bioorthogonal chemistry. Used in conjunction with the photo-cross-linking methodology, it serves as a sound strategy in the exploration of biological processes and beyond.
View Article and Find Full Text PDFBioorg Med Chem Lett
December 2024
Department of Chemistry, University of Southern California, Los Angeles, CA 90089, USA. Electronic address:
Carbohydrates play crucial roles in biological systems, including by mediating cell and protein interactions. The complexity and transient nature of carbohydrate-dependent interactions pose significant challenges for their characterization, as traditional techniques often fail to capture these low-affinity binding events. This review highlights the increasing utility of photocrosslinkers in studying carbohydrate-mediated interactions.
View Article and Find Full Text PDFMethods Mol Biol
December 2024
Heidelberg University Biochemistry Center, Heidelberg, Germany.
Functionalized lipid analogs are a versatile tool for studying lipid localization, metabolism and interactions in cells. As a common follow-up research, in vitro experiments are utilized to confirm specific interactors and characterize protein-lipid interactions. Here, we describe protocols that rely on commercially available photoactivatable and clickable lipids in reconstituted systems to capture protein-lipid interactions and detect lipid transport between purified proteins.
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