Recent progress in cancer cell membrane-based nanoparticles for biomedical applications

• Qixiong Lin,
• Yueyou Peng,
• Yanyan Wen,
• Xiaoqiong Li,
• Donglian Du,
• Weibin Dai,
• Wei Tian and
• Yanfeng Meng

Beilstein J. Nanotechnol. 2023, 14, 262–279, doi:10.3762/bjnano.14.24

• ). It also counteracts immune clearance by interacting with Ig-like lectin 10 (Siglec-10) expressed by macrophages [43]. Moreover, PD-L1 and B2M play an important role in preventing macrophage phagocytosis [43]. Most of the protein components can be efficiently retained and transferred to NPs during the

Nanotechnology – a robust tool for fighting the challenges of drug resistance in non-small cell lung cancer

• Filip Gorachinov,
• Fatima Mraiche,
• Diala Alhaj Moustafa,
• Ola Hishari,
• Yomna Ismail,
• Jensa Joseph,
• Maja Simonoska Crcarevska,
• Marija Glavas Dodov,
• Nikola Geskovski and
• Katerina Goracinova

Beilstein J. Nanotechnol. 2023, 14, 240–261, doi:10.3762/bjnano.14.23

Applications of superparamagnetic iron oxide nanoparticles in drug and therapeutic delivery, and biotechnological advancements

• Maria Suciu,
• Corina M. Ionescu,
• Alexandra Ciorita,
• Septimiu C. Tripon,
• Dragos Nica,
• Hani Al-Salami and
• Lucian Barbu-Tudoran

Beilstein J. Nanotechnol. 2020, 11, 1092–1109, doi:10.3762/bjnano.11.94

• negatively charged SPIONs [57], together with other weak binding proteins, i.e., mannose-binding lectin and their associated serine proteases, apolipoproteins, beta-2 glycoprotein, and clotting factors FXI and FXII. SPIONs with no surface charge have no proteins adsorbed onto them [58][59]. These

Multilayer capsules made of weak polyelectrolytes: a review on the preparation, functionalization and applications in drug delivery

• Varsha Sharma and
• Anandhakumar Sundaramurthy

Beilstein J. Nanotechnol. 2020, 11, 508–532, doi:10.3762/bjnano.11.41

• efficient carriers for controlled release. The later work on capsule/lipid systems incorporated with neoglycolipid or folate-linked lipid showed high affinity to lectin (concanavalin A) and breast cancer cells (MCF-7) [109]. The efficient delivery of the daunorubicin hydrochloride (DNR) anticancer drug to

• . For instance, the capsules incorporating a galactose branched polymer (PGEDMC) as one of the PE have shown specific recognition abilities with peanut agglutinin (PNA) lectin rather than nonspecific concanavalin A [111]. Although carbohydrate-related functionalization has been mostly explored for

Mannosylated brush copolymers based on poly(ethylene glycol) and poly(ε-caprolactone) as multivalent lectin-binding nanomaterials

• Stefania Ordanini,
• Wanda Celentano,
• Anna Bernardi and
• Francesco Cellesi

Beilstein J. Nanotechnol. 2019, 10, 2192–2206, doi:10.3762/bjnano.10.212

• , as investigated by concanavalin A binding assay. The results indicate that carbohydrate–lectin interactions can be tuned by the macromolecular architecture and functionality, hence the importance of these macromolecular properties in the design of targeted anti-pathogenic nanomaterials. Keywords

• : atom transfer radical polymerization (ATRP); glycopolymer; lectin; poly(ethylene glycol); poly(ε-caprolactone); ring-opening polymerization (ROP); Introduction Carbohydrate–protein interactions are involved in many biological processes, including cell recognition and cell–cell adhesion. These

• -functionalized monomer, starting from a four-arm initiator based on poly(ε-caprolactone), led to a library of glucose-functionalized aggregates able to bind the glucose- and mannose-binding lectin Concanavalin A (Con A) [12]. The combination of ATRP of protected alkyne monomers and a copper-catalyzed azide

The structural and chemical basis of temporary adhesion in the sea star Asterina gibbosa

• Birgit Lengerer,
• Marie Bonneel,
• Mathilde Lefevre,
• Elise Hennebert,
• Philippe Leclère,
• Emmanuel Gosselin,
• Peter Ladurner and
• Patrick Flammang

Beilstein J. Nanotechnol. 2018, 9, 2071–2086, doi:10.3762/bjnano.9.196

• adaptation to a benthic life on rocky intertidal areas. Lectin- and immuno-labelling indicated similarities but also some differences in adhesive composition between the two species. Further research on the temporary adhesive of A. gibbosa will allow the identification of conserved motifs in sea star

• meshwork was recently characterized and named sea star footprint protein-1 (Sfp1) [8]. Thirty-four additional proteins specific for footprints were identified and at least two were found to be glycosylated [28][29]. Additionally, lectin labelling of tube foot sections and footprints in A. rubens revealed

• interference microscopy, and atomic force microscopy (AFM). A. gibbosa tube feet and footprints were labelled with antibodies raised against the adhesive protein Sfp1 from A. rubens, but no cross-reactivity was observed. To detect carbohydrate moieties, we performed lectin labelling with 24 commercially

Review on nanoparticles and nanostructured materials: history, sources, toxicity and regulations

• Jaison Jeevanandam,
• Ahmed Barhoum,
• Yen S. Chan,
• Alain Dufresne and
• Michael K. Danquah

Beilstein J. Nanotechnol. 2018, 9, 1050–1074, doi:10.3762/bjnano.9.98

• and protein that are aligned in a column and layers of calcite, forms the thin and strong eggshell. During the eggshell formation, the CaCO3 NPs begin as an amorphous mineral which is transformed by the c-type lectin proteins into ordered crystals. The crystal transformation is initiated by the

Straightforward and robust synthesis of monodisperse surface-functionalized gold nanoclusters

• Silvia Varela-Aramburu,
• Richard Wirth,
• Chian-Hui Lai,
• Guillermo Orts-Gil and
• Peter H. Seeberger

Beilstein J. Nanotechnol. 2016, 7, 1278–1283, doi:10.3762/bjnano.7.118

• 2856 and 2925 cm−1. Apparently, all carbohydrates reacted as no S–H peaks were observed (Figure S11, Supporting Information File 1). Functional evidence for the formation of Glc-NC@Man was obtained by aggregating Glc-NC@Man with the addition of the mannose-binding lectin concanavalin A (ConA

• lectin ConA (4). Cell viability of Glc-NCs A) purified and B) without purification incubated for one day with L929 cells. The Glc-NCs were not toxic at any of the concentrations studied. C) Cellular uptake of Glc-NCs when incubated with L929 cells for one day. Gold concentration taken up by the cells was

Probing fibronectin–antibody interactions using AFM force spectroscopy and lateral force microscopy

• Andrzej J. Kulik,
• Małgorzata Lekka,
• Kyumin Lee,
• Grazyna Pyka-Fościak and
• Wieslaw Nowak

Beilstein J. Nanotechnol. 2015, 6, 1164–1175, doi:10.3762/bjnano.6.118

• experiment showing the effects of specific interaction forces using lateral force microscopy (LFM) was demonstrated for lectin–carbohydrate interactions some years ago. Such measurements are possible under the assumption that specific forces strongly dominate over the non-specific ones. However, obtaining

• –streptavidin [8], or lectin–carbohydrate [9]. Direct measurements of intermolecular forces for complementary DNA strands have been carried out as well [10]. Protein–antibody interactions are of particular interest in immunochemical-based diagnosis [11]. Therefore, studies of the interaction forces provide

• potential for performing such experiments in a much more effective way. The first attempt showing that specific interaction forces can be observed in the LFM signal has been applied to lectin–carbohydrate systems [24]. In that work, the specific interactions based on considerations of the frictional forces

Comparative evaluation of the impact on endothelial cells induced by different nanoparticle structures and functionalization

• Lisa Landgraf,
• Ines Müller,
• Peter Ernst,
• Miriam Schäfer,
• Christina Rosman,
• Isabel Schick,
• Oskar Köhler,
• Hartmut Oehring,
• Vladimir V. Breus,
• Thomas Basché,
• Carsten Sönnichsen,
• Wolfgang Tremel and
• Ingrid Hilger

Beilstein J. Nanotechnol. 2015, 6, 300–312, doi:10.3762/bjnano.6.28

• ) (LSM 510 Meta, Carl Zeiss Micro Imaging GmbH, Germany) and the cell nuclei were stained with Hoechst 33258 (Applichem, Germany) in blue. Further on, the glycocalyx was stained in red with lectin WGA-AlexaFluor633 (Invitrogen GmbH, Germany). Intracellular localisation of nanoparticles — electron

Coating with luminal gut-constituents alters adherence of nanoparticles to intestinal epithelial cells

• Heike Sinnecker,
• Katrin Ramaker and
• Andreas Frey

Beilstein J. Nanotechnol. 2014, 5, 2308–2315, doi:10.3762/bjnano.5.239

• grown on transwell filters (Figure 3A, B; counter-staining of the cell surface with a lectin). Pretreatment with the protein BSA appears to alleviate agglomeration as well as adherence. Only few distinct spots are visible on the cell surface, compared to a pronounced adherence of markedly larger

• lectin Ricinus communis agglutinin I (RCA I, Vector Laboratories, Burlingame, USA) to visualize the cell surface. Therefore the fixed cells were incubated with 50 mM NH4Cl in PBS (15 min at rt), washed again, and incubated with 0.2% gelatin in PBS (60 min at rt) to block nonspecific protein binding sites

• . The biotinylated lectin RCA I was used in a concentration of 20 µg/mL in 0.2% gelatin/PBS to label the cells over night at 4 °C. Afterwards the cells were incubated with Cy5-conjugated streptavidin (GE Healthcare, Brand Amersham, Pittsburgh, USA), 5 µg/mL in 0.2% gelatin/PBS, for 90 min at rt. Finally