Vitamin C is one of the most sensitive cosmetic active ingredients. To avoid its degradation, its encapsulation into biobased carriers such as dendrimers is one alternative of interest. In this work, we wanted to evaluate the potential of two biobased glycerodendrimer families (GlyceroDendrimers-Poly(AmidoAmine) (GD-PAMAMs) or GlyceroDendrimers-Poly(Propylene Imine) (GD-PPIs)) as a vitamin C carrier for topical application. The higher encapsulation capacity of GD-PAMAM-3 compared to commercial PAMAM-3 and different GD-PPIs, and its absence of cytotoxicity towards dermal cells, make it a good candidate. Investigation of its mechanism of action was done by using two kinds of biomimetic models of (SC), lipid monolayers and liposomes. GD-PAMAM-3 and VitC@GD-PAMAM-3 (GD-PAMAM-3 with encapsulated vitamin C) can both interact with the lipid representatives of the SC lipid matrix, whichever pH is considered. However, only pH 5.0 is suggested to be favorable to release vitamin C into the SC matrix. Their binding to SC-biomimetic liposomes revealed only a slight effect on membrane permeability in accordance with the absence of cytotoxicity but an increase in membrane rigidity, suggesting a reinforcement of the SC barrier property. Globally, our results suggest that the dendrimer GD-PAMAM-3 could be an efficient carrier for cosmetic applications.
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http://dx.doi.org/10.3390/molecules27228022 | DOI Listing |
Biophys J
January 2025
Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, Israel; Center for Physics and Chemistry of Living Systems, Tel Aviv University, Tel Aviv, Israel. Electronic address:
Migrasomes, the vesicle-like membrane micro-structures, arise on the retraction fibers (RFs), the branched nano-tubules pulled out of cell plasma membranes during cell migration and shaped by membrane tension. Migrasomes form in two steps: a local RF bulging is followed by a protein-dependent stabilization of the emerging spherical bulge. Here we addressed theoretically and experimentally the previously unexplored mechanism of bulging of membrane tubular systems.
View Article and Find Full Text PDFNat Commun
January 2025
Biomimetic Systems for Cell Engineering Laboratory, Institute for Bioengineering of Catalonia (IBEC), The Barcelona Institute of Science and Technology (BIST), Barcelona, Spain.
Intestinal epithelial cells are segregated into proliferative crypts and differentiated regions. This organization relies on specific signals, including Wnt3a, which regulates cell proliferation within crypts, and Eph/Ephrin, which dictates cell positioning along the crypt-villus axis. However, studying how the spatial distributions of these signals influences crypt-villus organization is challenging both in vitro and in vivo.
View Article and Find Full Text PDFSci Adv
January 2025
Department of Cardiac Surgery, Peking University Third Hospital, Beijing 100191, China.
Following myocardial infarction (MI), the accumulation of CD86-positive macrophages in the ischemic injury zone leads to secondary myocardial damage. Precise pharmacological intervention targeting this process remains challenging. This study engineered a nanotherapeutic delivery system with CD86-positive macrophage-specific targeting and ultrasound-responsive release capabilities.
View Article and Find Full Text PDFBiomater Sci
January 2025
Research Institute for Biomimetics and Soft Matter, Fujian Provincial Key Laboratory for Soft Functional Materials Research, Department of Physics, College of Physical Science and Technology, Xiamen University, Xiamen 361005, China.
Nature-inspired superhydrophobic materials have attracted considerable interest in blood-contacting biomedical applications due to their remarkable water-repellent and self-cleaning properties. However, the interaction mechanism between blood components and superhydrophobic surfaces remains unclear. To explore the effect of trapped air on platelet adhesion, we designed four distinct hydrophobic titanium dioxide (TiO) nanostructures with different fractions of trapped air.
View Article and Find Full Text PDFInorg Chem
January 2025
Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, United States.
The endogenous reduction of nitrite to nitrosyl is drawing increasing attention as a protective mechanism against hypoxic injury in mammalian physiology and as an alternative source of NO, which is involved in a wide variety of biological activities. Thus, chemical mechanisms for this transformation, which are mediated by metallo proteins, are of considerable interest. The study described here examines the reactions of the biomimetic models Co(TTP)(NO) (TTP = meso-tetratolylporphyrinato dianion) and Mn(TPP)(ONO) (TPP = meso-tetraphenyl-porphyrinato dianion) in sublimated solid films with hydrogen sulfide (HS) and with ethanethiol (EtSH) at various temperatures from 77 K to room temperature using in situ infrared and optical spectroscopy.
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