Lectins, glycoproteins with non-enzymatic and non-immunogenic origins, play essential roles in various biological processes. This study presents the purification and characterization of a lectin-like protein isolated from the seeds of Datura stramonium L., a member of the Solanaceae family. The purification of the lectin-like protein involved a dual method, employing both ammonium sulphate precipitation and anion exchange chromatography utilizing DEAE-Sepharose. Analysis via SDS-PAGE showed a distinct band, displaying an estimated molecular weight of approximately 30 kDa., indicative of the purified protein's homogeneity. Additionally, the purified protein exhibited hemagglutination activity towards human B and O red blood cells, underscoring its lectin-like properties. Periodic acid Schiff (PAS) staining confirmed the glycoprotein nature of the purified protein. Furthermore, its anti-proliferative activity against human cancer Caco-2 cell lines was evaluated through MTT assay, revealing promising results. This study elucidates the purification and characterization of a lectin-like protein from Datura stramonium L. seeds, providing valuable insights into its potential biological functions and diagnostic research applications.

Carbohydrate–lectin interactions are extremely specific as the lectin is capable of recognising monomeric and oligomeric sugars in a reversible manner. It has been known for a long time that lectins have antibacterial, antifungal, and insecticidal activities. Recently, it has been reported that many lectins can prevent the virus growth by interacting with the viral envelop surface glycoprotein. Spike protein, which is found on the surface of some enveloped viruses, is heavily mannosylated and will have strong affinity for mannose specific lectins. According to the findings, lectins have a high binding affinity for the glycans of the SARS-CoV-2 spike glycoprotein, which contains N-glycosylation sites. As a result, various lectins are being researched and developed as anti-viral agents. According to our in silico studies, the amino acid residues Asn487, Tyr489, Gln493, Lys417, and Tyr505 of the receptor binding domain (RBD) of SARS-CoV-2 formed an interaction with the model lectin Lablab purpureus lectin. Similar interaction for SARS-CoV-2 spike protein was observed with Griffithsin lectin (algal source) as well. These observations demonstrate that lectins could be one of the potential molecules for neutralising coronavirus infection. This review focuses on anti-viral lectins isolated and characterized from plants and algae (last 5 years) and showed anti-viral properties against HIV, Influenza, and coronaviruses.

Diabetes mellitus (DM) has spread across the globe, increasing the risk of obesity, cardiovascular disease, and other comorbidities. Despite substantial research into the development of diabetic treatments that are effective in lowering blood glucose levels, their efficiency is short-lived due to unpleasant side effects such as weight gain and hypoglycemia. The discovery of secondary metabolites in the prevention and treatment of diabetes and its complications has an incentive to take interest in plant-based medications, and enzyme inhibitors have the potential to aid in the treatment and management of DM. This study aims to isolate, characterize, and analyse the influence of berberine-like alkaloids from alcoholic Cardiospermum halicacabum extract in vitro and in silico, as a possible inhibitor of Dipeptidyl peptidase-IV (DPP-IV) and alpha-amylase, two essential enzymes involved in diabetes. The alkaloid from C. halicacabum was identified as berberine, with an m/z of 336.1263. Purified berberine inhibits DPP-IV with an IC50 of 16.328 +/- 1.344 mu M and inhibits a amylase by 72% at 10 mu g/mL. In-silico studies demonstrated that berberine was found to bind to the active site of both DPP-IV and alpha-amylase. The precise mechanism underlying the observation has to be researched further in order to investigate C. halicacabum's anti-diabetic effects and argue for its possible application as alternative medicine.

•RMLP from R. mucronata leaves were used as a stabilizer and disperser for the synthesis of RMLP-SeNPs.•Taguchi design method were applied to optimize the synthesis conditions of RMLP-SeNPs.•RMLP-SeNPs have an average size of 54.85 nm with spherical structure.•It showed excellent in vitro antioxidant and antibiofilm activities.

Lectins are carbohydrate-binding proteins broadly used in various therapeutic and biomedical applications. The variable affinity of lectins towards variety of carbohydrates has raised attention for the biologist to explore functional aspects of lectins. Lectins express specificity to simple carbohydrates for example mannose, lactose, sialic acid, complex glycan, and glycoproteins. Lectins are classified based on their sugar specificity and are used as a tool to study protein-carbohydrate interactions. Lectins are ubiquitous in nature and identified from all sources such as bacteria, fungi, algae, and animals. Plants are the most abundant source of lectins, and till now, more than three hundred lectins were characterized from plants. These are distributed to various parts of a plant according to their requirements and function. The physiological role of lectins in a plant is still not well understood. The overabundant presence of lectins in plant seeds and storage tissues indicated their role in plant development. Plant lectins shows a broad range of activities like antibacterial, antifungal, insecticidal, anticancerous, antileishmanial, antiviral, and anticoagulants. In this review, we aim to highlight the plant lectins classification and their application in various biological aspects.

The inhibition of phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha (PIK3CA) protein could be a promising treatment for breast cancer. In this regard, docking studies were accomplished on various functionalized organic molecules. Among them, several derivatives of quinazolin-4(1H)-one exhibited anti-breast cancer activity and satisfied the drug likeliness properties. Further, the in vitro inhibitory studies by a series of 2-(2-phenoxyquinolin-3-yl)-2,3-dihydroquinazolin-4(1H)-one molecules showed strong anti-cancer activity than the currently available drug, wortmannin. The MTT cytotoxicity assay was used to predict the anti-proliferative activity of these drugs against MCF-7 cancer cells by inhibiting the PIK3CA protein. The dose-dependent analysis showed a striking decrease in cancer cell viability at 24 h with inhibitory concentrations (IC50 ) of 3b, 3c, 3d, 3f and 3m are 15±1, 17±1, 8±1, 10±1 and 60±1 (nanomoles), respectively. This is the first report in the literature on the inhibition of PIK3CA protein by quinazolinone derivatives that can be used in the treatment of cancer. Quinazolinone analogs have the potential to be safe and economically feasible scaffolds if they are produced using a chemical technique that is both straightforward and amenable to modification. From the cancer research perspective, this study can eventually offer better care for cancer patients.

QDs after protein coronation can undergo sequential interaction with other pollutants which may alter the physiochemical property of the QDs and influence the stability of the corona proteins.

A novel lectin was isolated, purified and characterized from seeds of Entada rheedii using ammonium sulphate precipitation followed by lactose affinity chromatography.On SDS-PAGE, the purified Entadin lectin appeared as a single band (monomer in nature) with a molecular mass of approx.20 kDa both in reducing as well as in nonreducing conditions.Mass spectroscopic analysis confirms the molecular weight of Entadin lectin as 19333 Da.Entadin lectin showed highest titer value in agglutination against human blood group-B RBC and its Hemagglutination activity was inhibited by lactose, cellobiose, and galactose only.Periodic Acid Schiff's (PAS) stain confirmed the glycoprotein nature of Entadin lectin with an approx.5 % of carbohydrate content.The lectin is highly stable even after incubation at a wide range of temperatures (30 to 60 °C) and pH (6 to 10).Antiproliferative effect of Entadin lectin against lung cancer cells A549 and cervical cancer cells HeLa showed IC50 value of 38 µg/mL and 34 µg/mL and no anti-proliferative activity against normal cells.Cell morphological studies revealed that Entadin lectin induced apoptosis both in A549 and HeLa cancer cells which was confirmed by (AO/EB) and Hoechst (33258) nuclear counter staining.Further, Lectin was crystallized using the hangingdrop vapour-diffusion method with 30% PEG 8000 as precipitating agent, 0.2 M ammonium sulphate and 0.1 M sodium cacodylate pH 6.5.

A novel Entadin lectin was isolated, purified, and characterized from the seeds of Entada rheedii by ammonium sulfate precipitation, followed by lactose affinity chromatography. On sodium dodecyl sulfate polyacrylamide gel electrophoresis, the purified Entadin lectin appeared as a single band (monomeric in nature) with a molecular mass of approximately 20 kDa in both reducing and nonreducing conditions. Mass spectroscopic analysis confirms the molecular weight of Entadin lectin as 19,333 Da. Entadin lectin showed a highest titer value in agglutination against human blood group B red blood cells, and its hemagglutination activity was inhibited by lactose, cellobiose, and galactose. Periodic acid Schiff staining confirmed the glycoprotein nature of Entadin lectin with an approximately 5% carbohydrate content. This lectin is highly stable even after incubation at a wide range of temperatures (30-60 °C) and pHs (6-10). The antiproliferative effect of Entadin lectin against lung cancer cells A549 and cervical cancer cells HeLa showed IC50 values of 28 and 32 μg/mL, respectively, and no antiproliferative activity against normal cells was observed. Cell morphological studies revealed that Entadin lectin induced apoptosis in both A549 and HeLa cancer cells, which was confirmed by acridine orange/ethidium bromide and Hoechst (33258) nuclear counterstaining.

This work describes purification and characterisation of a monocot mannose-specific lectin from Hyacinth bulbs. The purified lectin has a molecular mass of ∼30kDa in reducing as well as in non-reducing SDS-PAGE. In hydrodynamic studies by Dynamic Light Scattering (DLS) showed that purified lectin was monomeric in nature with a molecular size of 2.38±0.03nm. Agglutination activity of purified lectin was confirmed by rabbit erythrocytes and its agglutination activity was inhibited by d-mannose and a glycoprotein (ovalbumin). Glycoprotein nature of purified lectin was confirmed by Periodic Acid Schiff's (PAS) stain. Purified lectin showed moderate pH and thermal stability by retaining hemagglutination activity from pH 6-8 and temperature up to 60°C. It also suppressed the growth of human colon cancer cells (Caco-2) and cervical cancer cells (HeLa) with IC50 values of 127μg/mL and 158μg/mL respectively, after 24-h treatment. Morphological studies of treated cells (Caco-2 and HeLa) with hyacinth lectin by AO/EB dual staining indicated that purified lectin is capable of inducing apoptosis.