Dataset Information

Physicochemical Properties and Antiherpetic Activity of κ-Carrageenan Complex with Chitosan.

ABSTRACT: Nanoparticles formation is one of the ways to modulate the physicochemical properties and enhance the activity of original polysaccharides. For this purpose, based on the polysaccharide of red algae, κ-carrageenan (κ-CRG), it polyelectrolyte complex (PEC), with chitosan, were obtained. The complex formation was confirmed by ultracentrifugation in a Percoll gradient, with dynamic light scattering. According to electron microscopy and DLS, PEC is dense spherical particles with sizes in the range of 150-250 nm. A decrease in the polydispersity of the initial CRG was detected after the PEC formation. Simultaneous exposure of Vero cells with the studied compounds and herpes simplex virus type 1 (HSV-1) showed that the PEC exhibited significant antiviral activity, effectively inhibiting the early stages of virus-cell interaction. A two-fold increase in the antiherpetic activity (selective index) of PEC compared to κ-CRG was shown, which may be due to a change in the physicochemical characteristics of κ-CRG in PEC.

SUBMITTER: Davydova VN

PROVIDER: S-EPMC10141160 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Physicochemical Properties and Antiherpetic Activity of κ-Carrageenan Complex with Chitosan.

Davydova Viktoriya N VN Krylova Natalya V NV Iunikhina Olga V OV Volod'ko Aleksandra V AV Pimenova Evgeniya A EA Shchelkanov Mikhail Y MY Yermak Irina M IM

Marine drugs 20230413 4

Nanoparticles formation is one of the ways to modulate the physicochemical properties and enhance the activity of original polysaccharides. For this purpose, based on the polysaccharide of red algae, κ-carrageenan (κ-CRG), it polyelectrolyte complex (PEC), with chitosan, were obtained. The complex formation was confirmed by ultracentrifugation in a Percoll gradient, with dynamic light scattering. According to electron microscopy and DLS, PEC is dense spherical particles with sizes in the range o ...[more]

PMID: 37103377

Similar Datasets

Project description:Algal cell wall polysaccharides constitute a large fraction in the biomass of marine primary producers and are thus important in nutrient transfer between trophic levels in the marine ecosystem. In order for this transfer to take place, polysaccharides must be degraded into smaller mono- and disaccharide units, which are subsequently metabolized, and key components in this degradation are bacterial enzymes. The marine bacterium Colwellia echini A3T is a potent enzyme producer since it completely hydrolyzes agar and κ-carrageenan. Here, we report that the genome of C. echini A3T harbors two large gene clusters for the degradation of carrageenan and agar, respectively. Phylogenetical and functional studies combined with transcriptomics and in silico structural modeling revealed that the carrageenolytic cluster encodes furcellaranases, a new class of glycoside hydrolase family 16 (GH16) enzymes that are key enzymes for hydrolysis of furcellaran, a hybrid carrageenan containing both β- and κ-carrageenan motifs. We show that furcellaranases degrade furcellaran into neocarratetraose-43-O-monosulfate [DA-(α1,3)-G4S-(β1,4)-DA-(α1,3)-G], and we propose a molecular model of furcellaranases and compare the active site architectures of furcellaranases, κ-carrageenases, β-agarases, and β-porphyranases. Furthermore, C. echini A3T was shown to encode κ-carrageenases, ι-carrageenases, and members of a new class of enzymes, active only on hybrid β/κ-carrageenan tetrasaccharides. On the basis of our genomic, transcriptomic, and functional analyses of the carrageenolytic enzyme repertoire, we propose a new model for how C. echini A3T degrades complex sulfated marine polysaccharides such as furcellaran, κ-carrageenan, and ι-carrageenan.IMPORTANCE Here, we report that a recently described bacterium, Colwellia echini, harbors a large number of enzymes enabling the bacterium to grow on κ-carrageenan and agar. The genes are organized in two clusters that encode enzymes for the total degradation of κ-carrageenan and agar, respectively. As the first, we report on the structure/function relationship of a new class of enzymes that hydrolyze furcellaran, a partially sulfated β/κ-carrageenan. Using an in silico model, we hypothesize a molecular structure of furcellaranases and compare structural features and active site architectures of furcellaranases with those of other GH16 polysaccharide hydrolases, such as κ-carrageenases, β-agarases, and β-porphyranases. Furthermore, we describe a new class of enzymes distantly related to GH42 and GH160 β-galactosidases and show that this new class of enzymes is active only on hybrid β/κ-carrageenan oligosaccharides. Finally, we propose a new model for how the carrageenolytic enzyme repertoire enables C. echini to metabolize β/κ-, κ-, and ι-carrageenan.

Dataset Information

Physicochemical Properties and Antiherpetic Activity of κ-Carrageenan Complex with Chitosan.

Publications

Physicochemical Properties and Antiherpetic Activity of κ-Carrageenan Complex with Chitosan.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets