Georgios Papadopoulos

Dr. Georgios Papadopoulos


Research Focus & Metrics

Academic Career Length

12Years (2015-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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Konstantinos FarsalinosKonstantinos Farsalinos
Konstantinos Farsalinos
EEElias Eliopoulos
Elias Eliopoulos
Demetres LeonidasDemetres Leonidas
Demetres Leonidas
GPGeorgios Papadopoulos
Georgios Papadopoulos
STSocrates Tzartos
Socrates Tzartos
Konstantinos PoulasKonstantinos Poulas
Konstantinos Poulas
While SARS-CoV-2 uses angiotensin converting enzyme 2 (ACE2) as the receptor for cell entry, it is important to examine other potential interactions between the virus and other cell receptors. Based on the clinical observation of low prevalence of smoking among hospitalized COVID-19 patients, we examined and identified a “toxin-like” amino acid (aa) sequence in the Receptor Binding Domain of the Spike Glycoprotein of SARS-CoV-2 (aa 375–390), which is homologous to a sequence of the Neurotoxin homolog NL1, one of the many snake venom toxins that are known to interact with nicotinic acetylcholine receptors (nAChRs). We present the 3D structural location of this “toxin-like” sequence on the Spike Glycoprotein and the superposition of the modelled structure of the Neurotoxin homolog NL1 and the SARS-CoV-2 Spike Glycoprotein. We also performed computational molecular modelling and docking experiments using 3D structures of the SARS-CoV-2 Spike Glycoprotein and the extracellular domain of the nAChR α9 subunit. We identified a main interaction between the aa 381–386 of the SARS-CoV-2 Spike Glycoprotein and the aa 189–192 of the extracellular domain of the nAChR α9 subunit, a region which forms the core of the “toxin-binding site” of the nAChRs. The mode of interaction is very similar to the interaction between the α9 nAChR and α-bungarotoxin. A similar interaction was observed between the pentameric α7 AChR chimera and SARS-CoV-2 Spike Glycoprotein. The findings raise the possibility that SARS-CoV-2 may interact with nAChRs, supporting the hypothesis of dysregulation of the nicotinic cholinergic system being implicated in the pathophysiology of COVID-19. Nicotine and other nicotinic cholinergic agonists may protect nAChRs and thus have therapeutic value in COVID-19 patients.

21 June 2015 in European Biophysics Journal
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SFStelios Floros
Stelios Floros
MLMaria Liakopoulou-Kyriakides
Maria Liakopoulou-Kyriakides
KKKostas Karatasos
Kostas Karatasos
GPGeorgios Papadopoulos
Georgios Papadopoulos

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SPStefanos Pendas
Stefanos Pendas
AAAntonis Asiminas
Antonis Asiminas
AKAlexandros Katranidis
Alexandros Katranidis
Costas TsioptsiasCostas Tsioptsias
Costas Tsioptsias
MPMaria Pitou
Maria Pitou
Theodora Choli-PapadopoulouTheodora Choli-Papadopoulou
Theodora Choli-Papadopoulou
Staphylococcus aureus is one of the major pathogens causing and spreading hospital acquired infections. Since it is highly resistant to new generation antibiotics, novel strategies have to be developed such as the construction of biofunctionalized non-adherent surfaces that will prevent its tethering and subsequent spread in the hospital environment. In this frame, the domain D of protein A (SpAD) of S. aureus has been immobilized onto cellulose acetate scaffolds by using the streptavidin/biotin interaction, in order to study its interaction with the A1 domain of von Willebrand factor (vWF A1), a protein essential for hemostasis, found in human plasma. Subsequently, the biofunctionalized cellulose acetate scaffolds were incubated with S. aureus in the presence and absence of vWF A1 at different time periods and their potential to inhibit S. aureus growth was studied with scanning electron microscopy (SEM). The SpAD biofunctionalized scaffolds perceptibly ameliorated the non-adherent properties of the material, and in particular, the interaction between SpAD and vWF A1 effectively inhibited the growth of S. aureus. Thus, the exhibition of significant non-adherent properties of scaffolds addresses their potential use for covering medical equipment, implants, and stents.

30 August 2016 in Molecules
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APAlexandros Priftis
Alexandros Priftis
DIMITRIOS STAGOSDIMITRIOS STAGOS
DIMITRIOS STAGOS
NTNikolaos Tzioumakis
Nikolaos Tzioumakis
KKKonstantinos Konstantinopoulos
Konstantinos Konstantinopoulos
APAnastasia Patouna
Anastasia Patouna
Dimitrios KouretasDimitrios Kouretas
Dimitrios Kouretas
Measuring the antioxidant capacity of foods is essential, as a means of quality control to ensure that the final product reaching the consumer will be of high standards. Despite the already existing assays with which the antioxidant activity is estimated, new, faster and low cost methods are always sought. Therefore, we have developed a novel colorimeter and combined it with a slightly modified DPPH assay, thus creating a kit that can assess the antioxidant capacity of liquids (e.g., different types of coffee, beer, wine, juices) in a quite fast and low cost manner. The accuracy of the colorimeter was ensured by comparing it to a fully validated Hitachi U-1900 spectrophotometer, and a coefficient was calculated to eliminate the observed differences. In addition, a new, user friendly software was developed, in order to render the procedure as easy as possible, while allowing a central monitoring of the obtained results. Overall, a novel kit was developed, with which the antioxidant activity of liquids can be measured, firstly to ensure their quality and secondly to assess the amount of antioxidants consumed with the respective food.