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  1. Article ; Online: The Impact of Nanomaterial Morphology on Modulation of Carbohydrate-Protein Interactions.

    Ravindra Bhoge, Preeti / Chandra, Ankita / Kikkeri, Raghavendra

    ChemMedChem

    2023  Volume 18, Issue 18, Page(s) e202300262

    Abstract: Carbohydrate-protein interactions (CPIs) play a crucial role in the regulation of various physiological and pathological processes within living systems. However, these interactions are typically weak, prompting the development of multivalent probes, ... ...

    Abstract Carbohydrate-protein interactions (CPIs) play a crucial role in the regulation of various physiological and pathological processes within living systems. However, these interactions are typically weak, prompting the development of multivalent probes, including nanoparticles and polymer scaffolds, to enhance the avidity of CPIs. Additionally, the morphologies of glyco-nanostructures can significantly impact protein binding, bacterial adhesion, cellular internalization, and immune responses. In this review, we have examined the advancements in glyco-nanostructures of different shapes that modulate CPIs. We specifically emphasize glyco-nanostructures constructed from small-molecule amphiphilic carbohydrates, block copolymers, metal-based nanoparticles, and carbon-based materials, highlighting their potential applications in glycobiology.
    MeSH term(s) Carbohydrates/pharmacology ; Carbohydrates/chemistry ; Nanostructures/chemistry ; Metal Nanoparticles/chemistry ; Polymers/chemistry ; Carbon
    Chemical Substances Carbohydrates ; Polymers ; Carbon (7440-44-0)
    Language English
    Publishing date 2023-07-19
    Publishing country Germany
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 2218496-X
    ISSN 1860-7187 ; 1860-7179
    ISSN (online) 1860-7187
    ISSN 1860-7179
    DOI 10.1002/cmdc.202300262
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Molecular recognition and proteoglycan mimic arrangement: modulating cisplatin toxicity.

    Anand, Saurabh / Mardhekar, Sandhya / Bhoge, Preeti Ravindra / Mishra, Sandeep Kumar / Kikkeri, Raghavendra

    Chemical communications (Cambridge, England)

    2024  Volume 60, Issue 33, Page(s) 4495–4498

    Abstract: We have demonstrated that cisplatin (CP), an anticancer drug, showed a preference for binding the sulfated-L-iduronic acid (S-L-IdoA) unit over the sulfated-D-glucuronic acid unit of heparan sulfate. The multivalency of S-L-IdoA, such as in the ... ...

    Abstract We have demonstrated that cisplatin (CP), an anticancer drug, showed a preference for binding the sulfated-L-iduronic acid (S-L-IdoA) unit over the sulfated-D-glucuronic acid unit of heparan sulfate. The multivalency of S-L-IdoA, such as in the proteoglycan mimic, resulted in distinct modes of cell-surface engineering in normal and cancer cells, with these disparities having a significant impact on CP-mediated toxicity.
    MeSH term(s) Proteoglycans ; Cisplatin ; Heparitin Sulfate/chemistry ; Glucuronic Acid/metabolism ; Iduronic Acid ; Sulfates
    Chemical Substances Proteoglycans ; Cisplatin (Q20Q21Q62J) ; Heparitin Sulfate (9050-30-0) ; Glucuronic Acid (8A5D83Q4RW) ; Iduronic Acid (3402-98-0) ; Sulfates
    Language English
    Publishing date 2024-04-18
    Publishing country England
    Document type Journal Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d4cc00464g
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: The Shape of Nanostructures Encodes Immunomodulation of Carbohydrate Antigen and Vaccine Development.

    Toraskar, Suraj / Madhukar Chaudhary, Preeti / Kikkeri, Raghavendra

    ACS chemical biology

    2022  Volume 17, Issue 5, Page(s) 1122–1130

    Abstract: Gold nanoparticles (AuNPs) have shown remarkable potential for vaccine development, but the influence of the size and shape of nanoparticles modulating the T-cell-dependent carbohydrate antigen processing and immunomodulation is poorly investigated. Here, ...

    Abstract Gold nanoparticles (AuNPs) have shown remarkable potential for vaccine development, but the influence of the size and shape of nanoparticles modulating the T-cell-dependent carbohydrate antigen processing and immunomodulation is poorly investigated. Here, we described how different shapes and sizes of gold nanostructures carrying adjuvant modulate carbohydrate-based antigen processing in murine dendritic cells (mDCs) and subsequent T-cell activation produce a robust antibody response. As a prototype, CpG-adjuvant-coated spherical and rod- and star-shaped AuNPs were conjugated to the tripodal Tn-glycopeptide antigen to study their DC uptake and activation of T-cells in a DCs/T-cell co-culture assay. Our results showed that the spherical and star-shaped AuNPs displayed relatively weak receptor-mediated uptake and endosomal sequestration; however, they induced a high level of T helper-1 (Th1) biasing immune responses compared with rod-shaped AuNPs. Furthermore, the
    MeSH term(s) Adjuvants, Immunologic/pharmacology ; Animals ; Antigen Presentation ; Carbohydrates ; Dendritic Cells ; Glycopeptides/pharmacology ; Gold/chemistry ; Immunomodulation ; Metal Nanoparticles/chemistry ; Mice ; Nanostructures ; Vaccine Development
    Chemical Substances Adjuvants, Immunologic ; Carbohydrates ; Glycopeptides ; Gold (7440-57-5)
    Language English
    Publishing date 2022-04-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1554-8937
    ISSN (online) 1554-8937
    DOI 10.1021/acschembio.1c00998
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Editorial: Glycoconjugates in vaccines and immunotherapeutics.

    Shivatare, Sachin / Sanjiv, Kumar / Kikkeri, Raghavendra / Adamo, Roberto

    Frontiers in immunology

    2022  Volume 13, Page(s) 941474

    MeSH term(s) Glycoconjugates ; Immunotherapy ; Vaccines
    Chemical Substances Glycoconjugates ; Vaccines
    Language English
    Publishing date 2022-08-04
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2022.941474
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Synergestic interplay of uronic acid and sulfation composition of heparan sulfate on molecular recognition to activity

    Bhoge, Preeti Ravindra / Raigawali, Rakesh / Mardhekar, Sandhya / Anand, Saurabh / Kikkeri, Raghavendra

    Carbohydrate Research. 2023 Oct., v. 532 p.108919-

    2023  

    Abstract: Heparan sulfate (HS) is ubiquitous polysaccharide on the surface of all mammalian cells and extracellular matrices. The incredible structural complexity of HS arises from its sulfation patterns and disaccharide compositions, which orchestrate a wide ... ...

    Abstract Heparan sulfate (HS) is ubiquitous polysaccharide on the surface of all mammalian cells and extracellular matrices. The incredible structural complexity of HS arises from its sulfation patterns and disaccharide compositions, which orchestrate a wide range of biological activities. Researchers have developed elegant synthetic methods to obtain well-defined HS oligosaccharides to understand the structure-activity relationship. These studies revealed that specific sulfation codes and uronic acid variants could synergistically modulate HS-protein interactions (HSPI). Additionally, the conformational flexibility of l-Iduronic acid, a uronic acid unit has emerged as a critical factor in fine-tuning the microenvironment to modulate HSPI. This review delineates how uronic acid composition in HS modulates protein binding affinity, selectivity, and biological activity. Finally, the significance of sulfated homo-oligo uronic acid as heparin mimics in drug development is also discussed.
    Keywords bioactive properties ; drug development ; heparan sulfate ; heparin ; mammals ; oligosaccharides ; research ; structure-activity relationships ; uronic acids ; Uronic acid ; Growth factors ; Chemokines ; Viral spike protein
    Language English
    Dates of publication 2023-10
    Publishing place Elsevier Ltd
    Document type Article ; Online
    ZDB-ID 1435-7
    ISSN 1873-426X ; 0008-6215
    ISSN (online) 1873-426X
    ISSN 0008-6215
    DOI 10.1016/j.carres.2023.108919
    Database NAL-Catalogue (AGRICOLA)

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  6. Article ; Online: Fluorescent glyco-gold nanocluster induced EGFR mediated targeting of cancer cells.

    Chandra, Ankita / Bhoge, Preeti Ravindra / K R, Remya / Shanthamurthy, Chethan D / Kikkeri, Raghavendra

    Chemical communications (Cambridge, England)

    2023  Volume 59, Issue 9, Page(s) 1213–1216

    Abstract: A lot of attention has been focused on the functionalization of carbohydrate ligands on specific sizes and shapes of gold nanoparticles (AuNPs), where ultrasmall fluorescent AuNPs have not been well explored for direct imaging. Herein, we have engineered ...

    Abstract A lot of attention has been focused on the functionalization of carbohydrate ligands on specific sizes and shapes of gold nanoparticles (AuNPs), where ultrasmall fluorescent AuNPs have not been well explored for direct imaging. Herein, we have engineered fluorescent gold nanoclusters with sulfated oligo-iduronic acid ligands (I34), which strongly bind to the HB-EGF receptor over FGF2, and regulate EGF receptor-mediated cancer cell homing in both two- and three-dimensional (2D and 3D) cell culture systems. These results offer a new practical and direct imaging tool for carbohydrate research.
    MeSH term(s) Gold/pharmacology ; Metal Nanoparticles ; Carrier Proteins ; Coloring Agents ; ErbB Receptors ; Carbohydrates ; Neoplasms/diagnostic imaging ; Neoplasms/drug therapy
    Chemical Substances Gold (7440-57-5) ; Carrier Proteins ; Coloring Agents ; ErbB Receptors (EC 2.7.10.1) ; Carbohydrates
    Language English
    Publishing date 2023-01-26
    Publishing country England
    Document type Journal Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d2cc06227e
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: A Cell-Culture Technique to Encode Glyco-Nanoparticles Selectivity.

    Subramani, Balamurugan / Chaudhary, Preeti Madhukar / Kikkeri, Raghavendra

    Chemistry, an Asian journal

    2021  Volume 16, Issue 23, Page(s) 3900–3904

    Abstract: Nanoparticles (NPs) embedded with bioactive ligands such as carbohydrates, peptides, and nucleic acid have emerged as a potential tool to target biological processes. Traditional in vitro assays performed under statistic conditions may result in non- ... ...

    Abstract Nanoparticles (NPs) embedded with bioactive ligands such as carbohydrates, peptides, and nucleic acid have emerged as a potential tool to target biological processes. Traditional in vitro assays performed under statistic conditions may result in non-specific outcome sometimes, mainly because of the sedimentation and self-assembly nature of NPs. Inverted cell-culture assay allows for flexible and accurate detection of the receptor-mediated uptake and cytotoxicity of NPs. By combining this technique with glyco-gold nanoparticles, cellular internalization and cytotoxicity were investigated. Regioselective glycosylation patterns and shapes of the NPs could tune the receptors' binding affinity, resulting in precise cellular uptake of gold nanoparticles (AuNPs). Two cell lines HepG2 and HeLa were probed with galactosamine-embedded fluorescent AuNPs, revealing significant differences in cytotoxicity and uptake mechanism in upright and invert in vitro cell-culture assay, high-specificity toward uptake, and allowing for a rapid screening and optimization technique.
    MeSH term(s) Antineoplastic Agents/chemistry ; Antineoplastic Agents/pharmacology ; Cell Culture Techniques ; Cell Proliferation/drug effects ; Drug Screening Assays, Antitumor ; Galactosamine/chemistry ; Galactosamine/pharmacology ; Gold/chemistry ; Gold/pharmacology ; HeLa Cells ; Hep G2 Cells ; Humans ; Molecular Structure ; Nanoparticles/chemistry ; Particle Size ; Tumor Cells, Cultured
    Chemical Substances Antineoplastic Agents ; Gold (7440-57-5) ; Galactosamine (7535-00-4)
    Language English
    Publishing date 2021-10-13
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 2233006-9
    ISSN 1861-471X ; 1861-4728
    ISSN (online) 1861-471X
    ISSN 1861-4728
    DOI 10.1002/asia.202101015
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Synergestic interplay of uronic acid and sulfation composition of heparan sulfate on molecular recognition to activity.

    Bhoge, Preeti Ravindra / Raigawali, Rakesh / Mardhekar, Sandhya / Anand, Saurabh / Kikkeri, Raghavendra

    Carbohydrate research

    2023  Volume 532, Page(s) 108919

    Abstract: Heparan sulfate (HS) is ubiquitous polysaccharide on the surface of all mammalian cells and extracellular matrices. The incredible structural complexity of HS arises from its sulfation patterns and disaccharide compositions, which orchestrate a wide ... ...

    Abstract Heparan sulfate (HS) is ubiquitous polysaccharide on the surface of all mammalian cells and extracellular matrices. The incredible structural complexity of HS arises from its sulfation patterns and disaccharide compositions, which orchestrate a wide range of biological activities. Researchers have developed elegant synthetic methods to obtain well-defined HS oligosaccharides to understand the structure-activity relationship. These studies revealed that specific sulfation codes and uronic acid variants could synergistically modulate HS-protein interactions (HSPI). Additionally, the conformational flexibility of l-Iduronic acid, a uronic acid unit has emerged as a critical factor in fine-tuning the microenvironment to modulate HSPI. This review delineates how uronic acid composition in HS modulates protein binding affinity, selectivity, and biological activity. Finally, the significance of sulfated homo-oligo uronic acid as heparin mimics in drug development is also discussed.
    MeSH term(s) Animals ; Uronic Acids ; Heparitin Sulfate/chemistry ; Oligosaccharides/chemistry ; Heparin/metabolism ; Protein Binding ; Mammals/metabolism
    Chemical Substances Uronic Acids ; Heparitin Sulfate (9050-30-0) ; Oligosaccharides ; Heparin (9005-49-6)
    Language English
    Publishing date 2023-08-03
    Publishing country Netherlands
    Document type Review ; Journal Article
    ZDB-ID 1435-7
    ISSN 1873-426X ; 0008-6215
    ISSN (online) 1873-426X
    ISSN 0008-6215
    DOI 10.1016/j.carres.2023.108919
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Surface-Controlled Sialoside-Based Biosensing of Viral and Bacterial Neuraminidases.

    Alshanski, Israel / Toraskar, Suraj / Gordon-Levitan, Daniel / Massetti, Marco / Jain, Prashant / Vaccaro, Luigi / Kikkeri, Raghavendra / Hurevich, Mattan / Yitzchaik, Shlomo

    Langmuir : the ACS journal of surfaces and colloids

    2024  Volume 40, Issue 14, Page(s) 7471–7478

    Abstract: Neuraminidases (NA) are sialic acid-cleaving enzymes that are used by both bacteria and viruses. These enzymes have sialoside structure-related binding and cleaving preferences. Differentiating between these enzymes requires using a large array of hard- ... ...

    Abstract Neuraminidases (NA) are sialic acid-cleaving enzymes that are used by both bacteria and viruses. These enzymes have sialoside structure-related binding and cleaving preferences. Differentiating between these enzymes requires using a large array of hard-to-access sialosides. In this work, we used electrochemical impedimetric biosensing to differentiate among several pathogene-related NAs. We used a limited set of sialosides and tailored the surface properties. Various sialosides were grafted on two different surfaces with unique properties. Electrografting on glassy carbon electrodes provided low-density sialoside-functionalized surfaces with a hydrophobic submonolayer. A two-step assembly on gold electrodes provided a denser sialoside layer on a negatively charged submonolayer. The synthesis of each sialoside required dozens of laborious steps. Utilizing the unique protein-electrode interaction modes resulted in richer biodata without increasing the synthetic load. These principles allowed for profiling NAs and determining the efficacy of various antiviral inhibitors.
    MeSH term(s) Sialic Acids/chemistry ; Neuraminidase/chemistry ; Neuraminidase/metabolism ; N-Acetylneuraminic Acid/chemistry ; Bacteria ; Biosensing Techniques
    Chemical Substances Sialic Acids ; Neuraminidase (EC 3.2.1.18) ; N-Acetylneuraminic Acid (GZP2782OP0)
    Language English
    Publishing date 2024-03-30
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2005937-1
    ISSN 1520-5827 ; 0743-7463
    ISSN (online) 1520-5827
    ISSN 0743-7463
    DOI 10.1021/acs.langmuir.3c03943
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: Rational designing of glyco-nanovehicles to target cellular heterogeneity.

    Jain, Prashant / Shanthamurthy, Chethan D / Chaudhary, Preeti Madhukar / Kikkeri, Raghavendra

    Chemical science

    2021  Volume 12, Issue 11, Page(s) 4021–4027

    Abstract: The aberrant expression of endocytic epidermal growth factor receptors (EGFRs) in cancer cells has emerged as a key target for therapeutic intervention. Here, we describe for the first time a state-of-the-art design for a heparan sulfate (HS) ... ...

    Abstract The aberrant expression of endocytic epidermal growth factor receptors (EGFRs) in cancer cells has emerged as a key target for therapeutic intervention. Here, we describe for the first time a state-of-the-art design for a heparan sulfate (HS) oligosaccharide-based nanovehicle to target EGFR-overexpressed cancer cells in cellular heterogeneity. An ELISA plate IC
    Language English
    Publishing date 2021-01-28
    Publishing country England
    Document type Journal Article
    ZDB-ID 2559110-1
    ISSN 2041-6539 ; 2041-6520
    ISSN (online) 2041-6539
    ISSN 2041-6520
    DOI 10.1039/d1sc00140j
    Database MEDical Literature Analysis and Retrieval System OnLINE

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