Graphene oxide–chloroquine conjugate induces DNA damage in A549 lung cancer cells through autophagy modulation

• Braham Dutt Arya,
• Sandeep Mittal,
• Prachi Joshi,
• Alok Kumar Pandey,
• Jaime E. Ramirez-Vick,
• Govind Gupta and
• Surinder P. Singh

Beilstein J. Nanotechnol. 2025, 16, 316–332, doi:10.3762/bjnano.16.24

• , including WNT, Notch, STAT 1/3, and NRF-2, respectively [20]. Graphene oxide nanosheets have been shown to selectively disrupt the cell membrane and cytoskeleton of cancer cells through activation of FAK-Rho-ROCK pathway and suppressed expression of integrin [21]. It has also been found that nuclear

Polymer lipid hybrid nanoparticles for phytochemical delivery: challenges, progress, and future prospects

• Iqra Rahat,
• Pooja Yadav,
• Aditi Singhal,
• Mohammad Fareed,
• Jaganathan Raja Purushothaman,
• Mohammed Aslam,
• Raju Balaji,
• Sonali Patil-Shinde and
• Md. Rizwanullah

Beilstein J. Nanotechnol. 2024, 15, 1473–1497, doi:10.3762/bjnano.15.118

• (i.e., IQN-iRGD-PLHNPs) to enhance anti-BC activity by active tumor targeting [121]. Coumarin-6 was tagged with the nanocarrier to investigate the cellular uptake potential. The developed targeted PLHNPs represented markedly enhanced cell uptake in MDA-MB-231 due to integrin receptor-mediated

• profiles. The cell culture studies indicated that the targeted PLHNPs showed much greater cell uptake in MDA-MB-435s cells by integrin receptor-medicated endocytosis than the non-targeted PLHNPs. The targeted PLHNPs showed a significant reduction in IC50 value (by ≈50%) compared to the non-targeted PLHNPs

Realizing active targeting in cancer nanomedicine with ultrasmall nanoparticles

• André F. Lima,
• Giselle Z. Justo and
• Alioscka A. Sousa

Beilstein J. Nanotechnol. 2024, 15, 1208–1226, doi:10.3762/bjnano.15.98

• demonstrated enhanced efficacy in both cell-line-derived and patient-derived in vivo tumor xenograft models (Figure 3D). 5.2 RGD peptide ligands/integrin receptors Liang et al. prepared luminescent AuNCs coated with c(RGDyC) in a one-pot synthesis (Figure 4A) [122]. The peptide comprised two functional parts

• : one part (Tyr and Cys residues) was responsible for reducing Au3+ into AuNCs, while the other part (RGD sequence) targeted αvβ3 integrin receptors. In murine models, the AuNCs were non-toxic and underwent renal clearance. Upon intravenous administration to 4T1 breast cancer tumor-bearing mice, the

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

• transmembrane glycoprotein VCAM-1 (CD106) on the surface of the breast cancer cell membrane mediates adhesion to leukocytes and the early stages of brain metastasis seeding by combining with integrin VLA-1 (α4β1) [51][71]. Utilizing the preferential accumulation of platelets and leukocytes at the site of brain

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

• include ανβ3 integrin, aminopeptidase N (CD13), lymphocyte homing receptor (CD44), programmed death ligand-1 (CD274), folate receptor protein, nucleolin receptor, epidermal growth factor receptor (EGFR), vascular endothelial growth factor receptor (VEGFR), human epidermal growth factor receptor 2 (HER2

• receptors. After binding to αvβ3 and αvβ5 integrin receptors in the tumor vasculature, iRDG is subsequently cleaved by cellular proteases to a fragment with a stronger affinity for the neuropilin-1 receptor. Neuropilin-1 receptor binding triggers extravasation and initiates deep tissue penetration

Bioselectivity of silk protein-based materials and their bio-inspired applications

• Hendrik Bargel,
• Vanessa T. Trossmann,
• Christoph Sommer and
• Thomas Scheibel

Beilstein J. Nanotechnol. 2022, 13, 902–921, doi:10.3762/bjnano.13.81

• interaction [9]. Generally, integrin-mediated interactions involve a complex series of events including activation, ligand binding, reorganization of the cytoskeleton, and adhesion [13]. In this context, integrin activation is regulated in response to signal cascades inside the cell known as an “inside-out

• ” process initiated by other cell surface receptors, such as chemokine receptors and selectins. The subsequent interaction with cytoplasmic factors leads to a conformational switch in the extracellular integrin binding region from a non-adhesive (inactive) to an adhesive state [19]. Moreover, adhesive

• interactions also include activation outside the cell (outside-in process) mediated by the cytosolic domains of the integrin α- and β-subunits. The recruitment of either leukocytes or platelets from the blood circulation are examples that require both signalling pathways [9]. Cells in their native tissue

Effects of substrate stiffness on the viscoelasticity and migration of prostate cancer cells examined by atomic force microscopy

• Xiaoqiong Tang,
• Yan Zhang,
• Jiangbing Mao,
• Yuhua Wang,
• Zhenghong Zhang,
• Zhengchao Wang and
• Hongqin Yang

Beilstein J. Nanotechnol. 2022, 13, 560–569, doi:10.3762/bjnano.13.47

• and disease development. Studies have shown that solid tumorigenesis and metastasis are often accompanied by abnormal ECM cross-linking, remodelling, and increased tissue stiffness [10]. Peng et al. observed that substrate stiffness directly activates integrin β1 and adherent spot kinase, accelerates

Micro- and nanotechnology in biomedical engineering for cartilage tissue regeneration in osteoarthritis

• Zahra Nabizadeh,
• Mahmoud Nasrollahzadeh,
• Hamed Daemi,
• Mohamadreza Baghaban Eslaminejad,
• Ali Akbar Shabani,
• Mehdi Dadashpour,
• Majid Mirmohammadkhani and
• Davood Nasrabadi

Beilstein J. Nanotechnol. 2022, 13, 363–389, doi:10.3762/bjnano.13.31

Engineered titania nanomaterials in advanced clinical applications

• Padmavati Sahare,
• Paulina Govea Alvarez,
• Juan Manual Sanchez Yanez,
• Gabriel Luna-Bárcenas,
• Samik Chakraborty,
• Sujay Paul and
• Miriam Estevez

Beilstein J. Nanotechnol. 2022, 13, 201–218, doi:10.3762/bjnano.13.15

• integrin clustering and focal adhesion development. In this context, Chen et al. employed the adsorption of functional proteins (bone morphogenetic protein 2 and sclerostin antibody) to modify TiO2 nanotube arrays to repair bone fractures [35]. The PC alters biodistribution, biological identity and

The nanomorphology of cell surfaces of adhered osteoblasts

• Christian Voelkner,
• Mirco Wendt,
• Regina Lange,
• Max Ulbrich,
• Martina Gruening,
• Susanne Staehlke,
• Barbara Nebe,
• Ingo Barke and
• Sylvia Speller

Beilstein J. Nanotechnol. 2021, 12, 242–256, doi:10.3762/bjnano.12.20

• . Such loosening and the subsequent retraction of lamellipodia towards the cell body has been shown for keratinocytes [35]. Either the attachment of the lamellipodium via integrin was not successful or such processes may serve the cell to attain flexibility of structures and thereby responsiveness

Key for crossing the BBB with nanoparticles: the rational design

• Sonia M. Lombardo,
• Marc Schneider,
• Akif E. Türeli and
• Nazende Günday Türeli

Beilstein J. Nanotechnol. 2020, 11, 866–883, doi:10.3762/bjnano.11.72

• targeting liposomal drug delivery system was then developed by conjugating peptide-22 and c(RGDfK), a ligand of integrin αvβ3 that showed ability to target glioma cells, to liposomes loaded with doxorubicin. This formulation was tested in vivo on an intracranial glioma-bearing mouse model. The nanocarrier

• recognizing the cell-penetrating peptide R8-dGR, which could bind to both integrin αvβ3 and neuropilin-I receptors, was used to functionalize liposomes [154]. This formulation was tested in vitro and in vivo on intracranial glioma-bearing mice. The R8-dGR-conjugated liposomes could cross the bEnd.3 (murine

Identification of physicochemical properties that modulate nanoparticle aggregation in blood

• Ludovica Soddu,
• Duong N. Trinh,
• Eimear Dunne,
• Dermot Kenny,
• Giorgia Bernardini,
• Ida Kokalari,
• Arianna Marucco,
• Marco P. Monopoli and
• Ivana Fenoglio

Beilstein J. Nanotechnol. 2020, 11, 550–567, doi:10.3762/bjnano.11.44

• mobilize intracellular Ca2+, which instigates platelet shape change, degranulation, and up-regulation of the adhesive function of another platelet surface receptor, integrin αIIbβ3 [35]. The active conformation of αIIbβ3 integrin can then bind fibrinogen, VWF and fibronectin with high affinity, allowing

• aggregation. However, in this case the effect is not due to the interaction with integrin, but it is a non-specific process due to the tendency of fibrinogen to form fibrils similar to fibrin. This tendency is a consequence of the specific fibrinogen arrangement onto surfaces, modulated by the surface

Poly(1-vinylimidazole) polyplexes as novel therapeutic gene carriers for lung cancer therapy

• Gayathri Kandasamy,
• Elena N. Danilovtseva,
• Vadim V. Annenkov and
• Uma Maheswari Krishnan

Beilstein J. Nanotechnol. 2020, 11, 354–369, doi:10.3762/bjnano.11.26

• formation in the cells clearly indicating the effect of VEGF inhibition. Earlier studies have shown that VEGF binds to α9β1 integrin on the cell surface, which mediates the formation and migration of endothelial cells through Src and focal adhesion kinase [34]. Therefore, the silencing of VEGF retards tube

Targeting strategies for improving the efficacy of nanomedicine in oncology

• Gonzalo Villaverde and
• Alejandro Baeza

Beilstein J. Nanotechnol. 2019, 10, 168–181, doi:10.3762/bjnano.10.16

• specifically to αβ-integrin, which is usually upregulated in many different tumoral cell lines such as breast, lung or fibroblast cancer cells, and also by the epithelial cells of the tumoral blood vessels [32][33]. Ruoshlati et al. have reported that the cyclic version of RGD, CRGDKGPDC (called iRGD), which

• is cyclized by the disulfide bridge between both terminal cysteines, exhibits significantly a higher tumour specificity than linear RGD [34]. iRGD works in a sequential manner, first it binds to αβ-integrin by the RGD sequence encrypted within the cyclic structure and then, the peptide is broken by

Nanoparticle delivery to metastatic breast cancer cells by nanoengineered mesenchymal stem cells

• Liga Saulite,
• Karlis Pleiko,
• Ineta Popena,
• Dominyka Dapkute,
• Ricardas Rotomskis and
• Una Riekstina

Beilstein J. Nanotechnol. 2018, 9, 321–332, doi:10.3762/bjnano.9.32

• overexpression of integrin receptors which mediate the uptake of NPs through integrin receptor mediated endocytosis [46]. Ex vivo injected MSCs have a relatively short lifespan within the body. On average, 24 h after the injection, these MSCs are relocated to the liver and spleen [47][48]. MSCs overexpress the

Liquid-crystalline nanoarchitectures for tissue engineering

• Baeckkyoung Sung and
• Min-Ho Kim

Beilstein J. Nanotechnol. 2018, 9, 205–215, doi:10.3762/bjnano.9.22

• tissue-derived biopolymers used in pharmaceutics, cosmetics and food industries, have a strong advantage as a cell scaffold material in that they harbor specific amino acid sequences (such as Arg–Gly–Asp) on which cell attachment occurs through the binding of transmembrane receptors (such as integrin

• colleagues [91][92][93][94]. Specifically, substrates of ordered rod-like viruses in the nematic phase have been utilized for directed 2D growth of cells. In this case, viruses are genetically modified to express integrin-binding motifs on their major coat proteins by using phage display techniques

• hydrogel composed of the aligned nanofibrils, enhanced cellular outgrowth was induced via augmented expression of integrin α1, which resulted in arteriogenesis and blood perfusion recovery in the mouse ischemia model. In another study, hydrogel films made of concentrated collagen type I showed regular

Nano- and microstructured materials for in vitro studies of the physiology of vascular cells

• Alexandra M. Greiner,
• Adria Sales,
• Hao Chen,
• Sarah A. Biela,
• Dieter Kaufmann and
• Ralf Kemkemer

Beilstein J. Nanotechnol. 2016, 7, 1620–1641, doi:10.3762/bjnano.7.155

• cytoskeleton system often by a signaling cascade initiated by integrin receptor activation [172][244][245][246][247]. Thus, one possible and likely scenario is the detection of the surface topography by cytoskeleton elements (in particular actin) and focal adhesions, and the probing of the topography by

• proliferation rate [277]. ECs: Differently regulated genes from cells on microstructures, in comparison to cells on flat surfaces, showed that endothelial cells on microgrooves down-regulated genes related to the cell cycle as well as their gene for β1 integrin [278]. In the future, it would be interesting to

Antitumor magnetic hyperthermia induced by RGD-functionalized Fe₃O₄ nanoparticles, in an experimental model of colorectal liver metastases

• Oihane K. Arriortua,
• Eneko Garaio,
• Borja Herrero de la Parte,
• Maite Insausti,
• Luis Lezama,
• Fernando Plazaola,
• Jose Angel García,
• Jesús M. Aizpurua,
• Maialen Sagartzazu,
• Mireia Irazola,
• Nestor Etxebarria,
• Ignacio García-Alonso,
• Alberto Saiz-López and
• José Javier Echevarria-Uraga

Beilstein J. Nanotechnol. 2016, 7, 1532–1542, doi:10.3762/bjnano.7.147

• (Figure 5). This fact could be explained by the special affinity of the RGD peptides adhered to the surface of our MNPs, for integrin αVβ3 [45][46]. It has been established that αVβ3, αVβ5 and αVβ1 integrins are membrane cell receptors related to angiogenesis and intercellular adhesion, and are

• overexpressed in some types of solid tumors [47]. So it could be suggested that αVβ3 integrin would be responsible for the special location of MNPs around the tumors. Pathological studies demonstrated that there was no relevant damage in hepatic tissue after exposure to the hyperthermia treatment. However

• indicates that MNPs could not avoid phagocytosis. The fact that MNPs could be found in the fibro-vascular tissue surrounding the tumors could be explained by the special affinity of the RGD peptides adhered to the surface of our MNPs for integrin αVβ3. The exposure of the animals to hyperthermia treatment

Atomic force microscopy as analytical tool to study physico-mechanical properties of intestinal cells

• Christa Schimpel,
• Oliver Werzer,
• Eleonore Fröhlich,
• Gerd Leitinger,
• Markus Absenger-Novak,
• Birgit Teubl,
• Andreas Zimmer and
• Eva Roblegg

Beilstein J. Nanotechnol. 2015, 6, 1457–1466, doi:10.3762/bjnano.6.151

• /receptors. Such adhesion receptors include members of the cadherin, immunglobulin, selectin, proteoglycan and integrin superfamilies [56]. They trigger signaling pathways, which are involved in cellular processes (e.g., cell survival, tissue organization, binding interactions, specificity of cell–cell

• interactions) [56][57][58]. However, the cell adhesion molecule α5β1 integrin exhibits a different distribution pattern in M cells compared to enterocytes. Enterocytes display integrin only on basolateral and lateral surfaces, whereas M cells express α5β1 integrin on the apical membrane [41]. It is known that

• this cell adhesion molecule assists not only transformation from enterocytes to M cells but also preferential uptake by M cells [59]. This suggests that the presence of α5β1 integrin on the apical surfaces of M cells is likely to be responsible for the enhanced adhesion properties obtained via AFM

Model systems for studying cell adhesion and biomimetic actin networks

• Dorothea Brüggemann,
• Johannes P. Frohnmayer and
• Joachim P. Spatz

Beilstein J. Nanotechnol. 2014, 5, 1193–1202, doi:10.3762/bjnano.5.131

• 10.3762/bjnano.5.131 Abstract Many cellular processes, such as migration, proliferation, wound healing and tumor progression are based on cell adhesion. Amongst different cell adhesion molecules, the integrin receptors play a very significant role. Over the past decades the function and signalling of

• be incorporated into lipid vesicles, too. We here review the mechanisms of integrin-mediated cell adhesion and recent advances in the field of minimal cells towards synthetic adhesion. We focus on reconstituting integrins into lipid structures for mimicking cell adhesion and on the incorporation of

• actin networks and talin into model cells. Keywords: actin network; cell adhesion; giant unilamellar vesicle; integrin; lipid bilayer; synthetic cell; protein reconstitution; talin; Review Introduction Since Hooke first described a biological cell in 1665 tremendous progress has been made in

Nanodiamond-DGEA peptide conjugates for enhanced delivery of doxorubicin to prostate cancer

• Amanee D Salaam,
• Patrick Hwang,
• Roberus McIntosh,
• Hadiyah N Green,
• Ho-Wook Jun and
• Derrick Dean

Beilstein J. Nanotechnol. 2014, 5, 937–945, doi:10.3762/bjnano.5.107

• tissues, the ND-DGEA conjugates were designed to distinguish between cells that overexpress α2β1 integrin, bone metastatic prostate cancers cells (PC3), and cells that do not, human mesenchymal stem cells (hMSC). Utilizing the ND-DGEA+DOX system, the efficacy of 1 µg/mL and 2 µg/mL DOX doses increased

• efficacy enhancement properties of NDs for targeted metastatic prostate cancer treatments has not been previously reported. Prostate cancers have been known to exhibit various aberrations, such as integrin α and β subunits, depending on the stage of progression. Integrin α and β subunits α6, β1, β3 and β6

• are up-regulated in metastatic cancers [29], while α2 is down-regulated initially then up-regulated as disease progresses [29][30]. High expression of the α2β1 integrin has been correlated with tumor progression in a number of cancers [31][32][33]. The α2β1 integrin is a receptor mainly for type I

Nanoglasses: a new kind of noncrystalline materials

• Herbert Gleiter

Beilstein J. Nanotechnol. 2013, 4, 517–533, doi:10.3762/bjnano.4.61

• indicate that the lateral spacing of individual integrin receptor-ligand bonds determines the strength of cellular adhesion. For spacings larger than about 90 nm focal contact formation was found to be inhibited and detachment forces were significantly smaller than for spacings below 50 nm. This seems to

• be so because integrin clustering and adhesion-induced arginine-glycine-aspatic acid (RGD) ligands depend on the local order of the ligand arrangement on the substrate if the average ligand spacing is above 70 nm. Adhesion is “turned off“ by RGD patterning above 70 nm and “turned on” below this