This work aimed at preparing new nanoscale assemblies based on an amphiphilic bio-esterified β-cyclodextrin (β-CD), substituted at the secondary face with n-decanoic fatty acid chains (β-CD-C), and monoolein (MO) as new carriers for parenteral drug delivery. Stable binary (β-CD-C/MO) and ternary (β-CD-C/MO/stabilizer) nanoscale assemblies close to 100nm in size were successfully prepared in water by the solvent displacement method. The generated nanoparticles were fully characterized by dynamic light scattering, transmission electron microscopy, small-angle X-ray scattering, residual solvent analysis, complement activation and the contribution of each formulation parameter was determined by principal component analysis. The β-CD-C units were shown to self-organize into nanoparticles with a hexagonal supramolecular packing that was significantly modulated by the molar ratio of the constituents and the presence of a steric or electrostatic stabilizer (DOPE-PEG or DOPA/POPA, respectively). Indeed, nanoparticles differing in morphology and in hexagonal lattice parameters were obtained while the co-existence of multiple mesophases was observed in some formulations, in particular for the β-CD-C/MO/DOPA and β-CD-C/MO/POPA systems. The mixed β-CD-C/MO/DOPE-PEG nanoparticles (49:49:2 in mol%) appeared to be the most suitable for use as a drug delivery system since they contained a very low amount of residual solvent and showed a low level of complement C3 activation.
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http://dx.doi.org/10.1016/j.ijpharm.2017.07.007 | DOI Listing |
Nanoscale
January 2025
Soft Matter Nanotechnology, Center for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance (BRTA), Paseo de Miramon 194, 20014, Donostia-San Sebastián, Spain.
Targeted delivery offers solutions for more efficient therapies with fewer side effects. Here, lipopeptides (LPs) prepared by conjugation of the nuclear-targeting peptide analogue H-YKQSHKKGGKKGSG-NH (NrTP6) and two lauric acid chains are used to encapsulate the chemotherapeutic agent doxorubicin (DX) through a solvent-exchange protocol. LPs spontaneously form nanosized rod-like assemblies in phosphate buffer.
View Article and Find Full Text PDFLangmuir
January 2025
Department of Chemistry, University of North Bengal, Raja Rammohanpur, Siliguri 734013, West Bengal, India.
Self-assembly of amino acids and short-peptide derivatives attracted significant curiosity worldwide due to their unique self-assembly process and wide variety of applications. Amino acid is considered one of the important synthons in supramolecular chemistry. Self-assembly processes and applications of unfunctionalized native amino acids have been less reported in the literature.
View Article and Find Full Text PDFNanoscale
January 2025
Zhejiang Provincial Key Laboratory of Utilization and Innovation of Silkworm and Bee Resources, Institute of Applied Bioresource Research, College of Animal Science, Zhejiang University, Yuhangtang Road 866, Hangzhou, 310058 Zhejiang, P. R. China.
Gold nanorods (AuNRs) have shown great potential as photothermal agents for cancer therapy. However, the biosafety of AuNRs ordinarily synthesized using a cationic ligand assistance procedure has always been a subject of controversy, which limits their application in tumor therapy. In this study, we propose a novel strategy to enhance the biocompatibility of AuNRs by constructing a biological coating derived from silk fibroin (SF) on their surface.
View Article and Find Full Text PDFMater Today Bio
February 2025
Department of Chemical Engineering, Ben-Gurion University of the Negev, Beer Sheva, 8410501, Israel.
Protein-based biomaterials are in high demand due to their high biocompatibility, non-toxicity, and biodegradability. In this study, we explore the bacterial secreted protein A (EspA), which self-assembles into long extracellular filaments, as a potential building block for new protein-based biomaterials. We investigated the morphological and mechanical properties of EspA filaments and how protein engineering can modify them.
View Article and Find Full Text PDFJ Phys Chem B
January 2025
Department of Engineering Mechanics, KTH Royal Institute of Technology, 100 44 Stockholm, Sweden.
We here explore confinement-induced assembly of whey protein nanofibrils (PNFs) into microscale fibers using microfocused synchrotron X-ray scattering. Solvent evaporation aligns the PNFs into anisotropic fibers, and the process is followed in situ by scattering experiments within a droplet of PNF dispersion. We find an optimal temperature at which the order parameter of the protein fiber is maximized, suggesting that the degree of order results from a balance between the time scales of the forced alignment and the rotational diffusion of the fibrils.
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