The role of bacterial exopolysaccharides (EPS) in the synthesis of antimicrobial silver nanomaterials: A state-of-the-art review.

The emergence of multi-drug resistant (MDR) pathogens poses a significant global health concern due to the failure of conventional medical treatment. As a result, the development of several metallic (Ag, Au, Zn, Ti, etc.) nanoparticles, has gained prominence as an alternative to conventional antimicrobial therapies. Among these, green-synthesized silver nanoparticles (AgNPs) have gained significant attention due to their notable efficiency and broad spectrum of antimicrobial activity. Bacterial exopolysaccharides (EPS) have recently emerged as a promising biological substrate for the green synthesis of AgNPs. EPS possess polyanionic functional groups (hydroxyl, carboxylic, sulfate, and phosphate) that effectively reduce and stabilize AgNPs. EPS-mediated AgNPs exhibit a wide range of antimicrobial activity against various pathogenic microbes, including Gram-positive and Gram-negative bacteria, as well as fungi. The extraction and purification of bacterial EPS play a vital role in obtaining high-quality and -quantity EPS for industrial applications. This study focuses on the comprehensive methodology of EPS extraction and purification, encompassing screening, fermentation optimization, pretreatment, protein elimination, precipitation, and purification. The review specifically highlights the utilization of bacterial EPS-mediated AgNPs, covering EPS extraction, the synthesis mechanism of green EPS-mediated AgNPs, their characterization, and their potential applications as antimicrobial agents against pathogens. These EPS-mediated AgNPs offer numerous advantages, including biocompatibility, biodegradability, non-toxicity, and eco-friendliness, making them a promising alternative to traditional antimicrobials and opening new avenues in nanotechnology-based approaches to combat microbial infections.

Use of Spectroscopic Techniques to Reveal the Nature of the Interactions of Two Sialic Acid Specific Lectins with Gold Nanoparticles.

From UV-vis absorption, steady state and time resolved fluorescence measurements coupled with circular dichroism (CD) spectral studies, it was revealed that among the two lectins: Sambucus nigra agglutinin (SNA) and Saraca indica (saracin II), SNA forms stronger binding complex in the ground state with gold nanoparticles (GNPs). From the measurements of Stern-Volmer (SV) constants Ksv, and binding constants K(A) and number of binding sites two important inferences could be drawn. Firstly, the fluorescence quenching is primarily due to static quenching and secondly SNA forms stronger binding with GNPs relative to the other lectin saracin II. Synchronous fluorescence spectral measurements further substantiate this proposition of exhibiting the fully exposed tryptophan residue in case of SNA. It appears that the lectin SNA adopted a relatively looser conformation with the extended polypeptide structures leading to the exposure of the hydrophobic cavities which favoured stronger binding with GNPs. CD measurements demonstrate that gold nanoparticles when interact with the lectins (glycoproteins), no significant distortion in the structural pattern of the later occurs. The unaltered identity in the secondary structural pattern of both SNA and saracin II in presence of gold nanoparticles hints that GNPs may be used as useful drug or drug delivery systems.

A glucose/mannose binding lectin from litchi (Litchi chinensis) seeds: Biochemical and biophysical characterizations.

BACKGROUND: Lectins are highly important biomolecules to study several biological processes. A novel α-D-glucose/mannose specific lectin was isolated from the seeds of litchi fruits (Litchi chinensis) and its various biophysical and biochemical properties were studied. METHODS: Purification was done by successive Sephadex G 100 and Con A-Sepharose 4B affinity chromatography. SDS-PAGE, Surface Plasmon Resonance (SPR), steady state absorbance, fluorescence, time-correlated single-photon counting, circular dichroism and antibiofilm activity by measuring total protein estimation and azocasein degradation assay have been performed. RESULTS: The purified lectin is a homodimer of molecular mass ~ 54 kDa. The amount of lectin required for hemagglutination of normal human O erythrocytes was 6.72 µg/ml. Among the saccharides tested, Man-α-(1,6)-Man was found to be the most potent inhibitor (0.01 mM) determined by hemagglutination inhibition assay. Steady state and time resolved fluorescence measurements revealed that litchi lectin formed ground state complex with maltose (Ka=4.9 (±0.2)×104 M-1), which indicated static quenching (Stern-Volmer (SV) constant Ksv=4.6 (±0.2)×104 M-1). CD measurements demonstrated that litchi lectin showed no overall conformational change during the binding process with maltose. The lectin showed antibiofilm activity against Pseudomonus aeruginosa. CONCLUSIONS: A novel homodimeric lectin has been purified from the seeds of litchi fruits (Litchi chinensis) having specificity for α-d-glucose/mannose. The thermodynamics and conformational aspects of its interaction with maltose have been studied in detail. The antibiofilm activity of this lectin towards Pseudomonus aeruginosa has been explored. GENERAL SIGNIFICANCE: The newly identified litchi lectin is highly specific for α-d-glucose/mannose with an important antibiofilm activity towards Pseudomonus aeruginosa.

FeCl3 mediated arylidenation of carbohydrates.

Glycosides and thioglycosides based on monosaccharides in reaction with benzaldehyde dimethylacetal or p-methoxybenzaldehyde dimethyl acetal undergo FeCl(3)-catalyzed (20 mol%) regioselective 4,6-O-arylidenation producing the corresponding acetals in high yields. FeCl(3) also mediates acetalation of glycosides and thioglycosides of cellobiose, maltose, and lactose affording the corresponding 4',6'-O-benzylidene acetals, which were isolated after their acetylation in situ with acetic anhydride and pyridine. The combined yields (two steps) of these final products are also high (61-84%). The procedure is applicable to a wide variety of functional groups including -OBn.