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Intelligent Nanomaterials for Medicine: Carrier Platforms and Targeting Strategies—State of the Art
Published in Lajos P. Balogh, Nano-Enabled Medical Applications, 2020
Georgette B. Salieb-Beugelaar, Marc Wolf, Roman Lehner, Kegang Liu, Stephan Marsch, Patrick Hunziker
Peptides can have lipophilic or hydrophilic properties based on their amino acid composition and can therefore be used to construct amphiphilic molecules that form nanostructures by self-assembly [132–134]. Design considerations of these biopolymers for drug carriers are similar to other biocompatible polymers, but should take into account that peptides may act as strong immunogens and that the body already contains several lines of defense against foreign proteins and peptidic structures like virus capsids. In addition, a variety of peptidases exist in the body; if a system is preclinically developed for later clinical use in man, species differences in peptidase expression needs to be carefully considered. Virus self-assembly can act as an inspiration to build hollow or solid peptidic nanostructures [135, 136]. Bawa et al. showed enhanced cellular delivery and activity of the anticancer drug ellipticine to human lung carcinoma A549 cells using self-assembling peptide-based nanoparticles [137]. Naskar et al. presented the formation of multivesicular structures from self-assembling peptides, depicting sensitivity upon exposure to calcium ions leading to vesicular disruption. This intelligent sensing/switching functionality, allows cargo release suited for medically relevant payloads [138]. However, a natural extension of peptide-based systems is the exploitation of biologic peptide functions like their use as receptor ligands or enzymatic activity, naturally leading to nanomaterials with complex or switchable functionalities. Clinically, peptidic systems have entered clinical trials dominantly as nanoplatforms for vaccines offering multivalency as a potent immune system stimulant.
Unique enantiopure camphor-based neutral arene–ruthenium(II) complexes: DNA/BSA binding, kinetic and cytotoxic studies
Published in Journal of Coordination Chemistry, 2022
Milan M. Milutinović, Angelina Z. Caković, Dušan Ćoćić, Eduard Rais, Roland Schoch, Bojana Simović Marković, Nebojša Arsenijević, Vladislav Volarević, Snezana Jovanović-Stević, Jovana V. Bogojeski, René Wilhelm
Complexes 1 and 2 were docked into the DNA fragments representing either: (i) canonical B-DNA (PDB 1BNA) or (ii) DNA with an intercalation gap (PDB 1Z3F). 1BNA is the crystal structure of a synthetic DNA dodecamer, while 1Z3F is the crystal structure of a 6 bp DNA fragment in a complex with an intercalating anticancer drug, ellipticine. The best-docked poses with DNA are displayed in Figures 7 and 8, with the top-ranked poses according to used scoring functions displayed in Table 5. Based on docking results, 2 shows a better ability to dock into selected DNA fragments compared to 1. By comparing the results from different binding modes, both complexes are better docked in the DNA fragment presenting an intercalation gap (PDB ID: 1Z3F).