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  1. Article ; Online: Production of isotopically enriched high molecular weight hyaluronic acid and characterization by solid-state NMR.

    Rampratap, Pushpa / Lasorsa, Alessia / Perrone, Barbara / van der Wel, Patrick C A / Walvoort, Marthe T C

    Carbohydrate polymers

    2023  Volume 316, Page(s) 121063

    Abstract: Hyaluronic acid (HA) is a naturally occurring polysaccharide that is abundant in the extracellular matrix (ECM) of all vertebrate cells. HA-based hydrogels have attracted great interest for biomedical applications due to their high viscoelasticity and ... ...

    Abstract Hyaluronic acid (HA) is a naturally occurring polysaccharide that is abundant in the extracellular matrix (ECM) of all vertebrate cells. HA-based hydrogels have attracted great interest for biomedical applications due to their high viscoelasticity and biocompatibility. In both ECM and hydrogel applications, high molecular weight (HMW)-HA can absorb a large amount of water to yield matrices with a high level of structural integrity. To understand the molecular underpinnings of structural and functional properties of HA-containing hydrogels, few techniques are available. Nuclear magnetic resonance (NMR) spectroscopy is a powerful tool for such studies, e.g.
    MeSH term(s) Hyaluronic Acid/chemistry ; Molecular Weight ; Proteins/chemistry ; Magnetic Resonance Spectroscopy ; Hydrogels/chemistry
    Chemical Substances Hyaluronic Acid (9004-61-9) ; Proteins ; Hydrogels
    Language English
    Publishing date 2023-05-29
    Publishing country England
    Document type Journal Article
    ZDB-ID 1501516-6
    ISSN 1879-1344 ; 0144-8617
    ISSN (online) 1879-1344
    ISSN 0144-8617
    DOI 10.1016/j.carbpol.2023.121063
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  2. Article ; Online: Combinations of arginine and pullulan reveal the selective effect of stabilization mechanisms on different lyophilized proteins.

    T T Nguyen, Khanh / Zillen, Daan / Lasorsa, Alessia / van der Wel, Patrick C A / Frijlink, Henderik W / L J Hinrichs, Wouter

    International journal of pharmaceutics

    2024  Volume 654, Page(s) 123938

    Abstract: The stability of lactate dehydrogenase (LDH) and β-galactosidase (β-gal), incorporated in arginine/pullulan (A/P) mixtures at various weight ratios by lyophilization, was determined. The physicochemical characteristics of various A/P mixtures were ... ...

    Abstract The stability of lactate dehydrogenase (LDH) and β-galactosidase (β-gal), incorporated in arginine/pullulan (A/P) mixtures at various weight ratios by lyophilization, was determined. The physicochemical characteristics of various A/P mixtures were assessed. With decreasing A/P ratios, the glass transition temperature of the formulations increased. Furthermore, arginine crystallization due to high relative humidity (RH) exposure was prevented at an A/P weight ratio of 4/6 or less. When stored at 0 % RH / 60 °C for 4 weeks, arginine was superior to pullulan as stabilizer. During storage at 43 % RH / 30 ℃ for 4 weeks, the enzymatic activity of LDH was best retained at an A/P weight ratio of 2/8, while β-gal activity was relatively well-retained at A/P weight ratios of both 8/2 and 2/8. LDH seemed to be more prone to degradation in the rubbery state. In the glassy state, β-gal degraded faster than LDH. Solid-state nuclear magnetic resonance spectroscopy showed that (labeled) arginine experienced a different interaction in the two protein samples, reflecting a modulation of long-range correlations of the arginine side chain nitrogen atoms (Nε, Nη). In summary, LDH stabilization in the A/P matrix requires vitrification. Further stabilization difference between LDH and β-gal may be dependent on the interaction with arginine.
    MeSH term(s) Arginine/chemistry ; Proteins/chemistry ; Glucans ; L-Lactate Dehydrogenase/chemistry ; Freeze Drying/methods ; Drug Stability
    Chemical Substances pullulan (8ZQ0AYU1TT) ; Arginine (94ZLA3W45F) ; Proteins ; Glucans ; L-Lactate Dehydrogenase (EC 1.1.1.27)
    Language English
    Publishing date 2024-02-24
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 428962-6
    ISSN 1873-3476 ; 0378-5173
    ISSN (online) 1873-3476
    ISSN 0378-5173
    DOI 10.1016/j.ijpharm.2024.123938
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1409: Show issues Location:
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  3. Article ; Online: Production of isotopically enriched high molecular weight hyaluronic acid and characterization by solid-state NMR

    Rampratap, Pushpa / Lasorsa, Alessia / Perrone, Barbara / van der Wel, Patrick C.A. / Walvoort, Marthe T.C.

    Carbohydrate Polymers. 2023 May 29, p.121063-

    2023  , Page(s) 121063–

    Abstract: Hyaluronic acid (HA) is a naturally occurring polysaccharide that is abundant in the extracellular matrix (ECM) of all vertebrate cells. HA-based hydrogels have attracted great interest for biomedical applications due to their high viscoelasticity and ... ...

    Abstract Hyaluronic acid (HA) is a naturally occurring polysaccharide that is abundant in the extracellular matrix (ECM) of all vertebrate cells. HA-based hydrogels have attracted great interest for biomedical applications due to their high viscoelasticity and biocompatibility. In both ECM and hydrogel applications, high molecular weight (HMW)-HA can absorb a large amount of water to yield matrices with a high level of structural integrity. To understand the molecular underpinnings of structural and functional properties of HA-containing hydrogels, few techniques are available. Nuclear magnetic resonance (NMR) spectroscopy is a powerful tool for such studies, e.g. ¹³C NMR measurements can reveal the structural and dynamical features of (HMW) HA. However, a major obstacle to ¹³C NMR is the low natural abundance of ¹³C, necessitating the generation of HMW-HA that is enriched with ¹³C isotopes. Here we present a convenient method to obtain ¹³C- and ¹⁵N-enriched HMW-HA in good yield from Streptococcus equi subsp. zooepidemicus. The labeled HMW-HA has been characterized by solution and magic angle spinning (MAS) solid-state NMR spectroscopy, as well as other methods. These results will open new ways to study the structure and dynamics of HMW-HA-based hydrogels, and interactions of HMW-HA with proteins and other ECM components, using advanced NMR techniques.
    Keywords biocompatibility ; extracellular matrix ; hyaluronic acid ; hydrogels ; molecular weight ; nuclear magnetic resonance spectroscopy ; vertebrates ; viscoelasticity ; Solid-state NMR spectroscopy ; Isotopic enrichment ; Mass spectrometry
    Language English
    Dates of publication 2023-0529
    Publishing place Elsevier Ltd
    Document type Article ; Online
    Note Pre-press version
    ZDB-ID 1501516-6
    ISSN 1879-1344 ; 0144-8617
    ISSN (online) 1879-1344
    ISSN 0144-8617
    DOI 10.1016/j.carbpol.2023.121063
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  4. Article ; Online: Magnetic resonance investigation of conformational responses of tau protein to specific phosphorylation.

    Lasorsa, Alessia / Merzougui, Hamida / Cantrelle, François-Xavier / Sicoli, Giuseppe / Dupré, Elian / Hanoulle, Xavier / Belle, Valérie / Smet-Nocca, Caroline / Landrieu, Isabelle

    Biophysical chemistry

    2023  Volume 305, Page(s) 107155

    Abstract: Intrinsically disordered proteins (IDPs) are known to adopt many rapidly interconverting structures, making it difficult to pinpoint the specific conformational states that are relevant for their function. Tau is an important IDP, and its conformation is ...

    Abstract Intrinsically disordered proteins (IDPs) are known to adopt many rapidly interconverting structures, making it difficult to pinpoint the specific conformational states that are relevant for their function. Tau is an important IDP, and its conformation is known to be affected by post-translational modifications (PTMs), such as phosphorylation. To investigate the effect of specific phosphorylation on full-length Tau's dynamic global conformation, we employed a combination of nuclear magnetic resonance-based paramagnetic relaxation interference methods and electron paramagnetic resonance spectroscopy. By reproducing the AT8 epitope, comprising exclusive phosphorylation at residues S202 and T205, we were able to identify conformations specific to phosphorylated Tau, which exhibited a tendency towards less compact states. These mechanistic details are of significance to understand the path leading from soluble Tau to the ordered structure of Tau fibers. This approach proved to be successful for studying the conformational changes of (phosphorylated) full-length Tau and can potentially be extended to the study of other IDPs that undergo various PTMs.
    MeSH term(s) Phosphorylation ; tau Proteins/chemistry ; Magnetic Resonance Spectroscopy ; Protein Conformation ; Electron Spin Resonance Spectroscopy ; Intrinsically Disordered Proteins/chemistry ; Nuclear Magnetic Resonance, Biomolecular
    Chemical Substances tau Proteins ; Intrinsically Disordered Proteins
    Language English
    Publishing date 2023-12-14
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 185052-0
    ISSN 1873-4200 ; 0301-4622
    ISSN (online) 1873-4200
    ISSN 0301-4622
    DOI 10.1016/j.bpc.2023.107155
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    Zs.A 1147: Show issues Location:
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  5. Article ; Online: Photocontrol of the β-Hairpin Polypeptide Structure through an Optimized Azobenzene-Based Amino Acid Analogue.

    Parlato, Raffaella / Volarić, Jana / Lasorsa, Alessia / Bagherpoor Helabad, Mahdi / Kobauri, Piermichele / Jain, Greeshma / Miettinen, Markus S / Feringa, Ben L / Szymanski, Wiktor / van der Wel, Patrick C A

    Journal of the American Chemical Society

    2024  Volume 146, Issue 3, Page(s) 2062–2071

    Abstract: A family of neurodegenerative diseases, including Huntington's disease (HD) and spinocerebellar ataxias, are associated with an abnormal polyglutamine (polyQ) expansion in mutant proteins that become prone to form amyloid-like aggregates. Prior studies ... ...

    Abstract A family of neurodegenerative diseases, including Huntington's disease (HD) and spinocerebellar ataxias, are associated with an abnormal polyglutamine (polyQ) expansion in mutant proteins that become prone to form amyloid-like aggregates. Prior studies have suggested a key role for β-hairpin formation as a driver of nucleation and aggregation, but direct experimental studies have been challenging. Toward such research, we set out to enable spatiotemporal control over β-hairpin formation by the introduction of a photosensitive β-turn mimic in the polypeptide backbone, consisting of a newly designed azobenzene derivative. The reported derivative overcomes the limitations of prior approaches associated with poor photochemical properties and imperfect structural compatibility with the desired β-turn structure. A new azobenzene-based β-turn mimic was designed, synthesized, and found to display improved photochemical properties, both prior and after incorporation into the backbone of a polyQ polypeptide. The two isomers of the azobenzene-polyQ peptide showed different aggregate structures of the polyQ peptide fibrils, as demonstrated by electron microscopy and solid-state NMR (ssNMR). Notably, only peptides in which the β-turn structure was stabilized (azobenzene in the
    MeSH term(s) Humans ; Peptides/chemistry ; Azo Compounds ; Neurodegenerative Diseases ; Huntington Disease/metabolism ; Amino Acids
    Chemical Substances azobenzene (F0U1H6UG5C) ; Peptides ; Azo Compounds ; Amino Acids
    Language English
    Publishing date 2024-01-16
    Publishing country United States
    Document type Journal Article
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/jacs.3c11155
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  6. Article: Solid-state NMR spectroscopy insights for resolving different water pools in alginate hydrogels

    El Nokab, Mustapha El Hariri / Lasorsa, Alessia / Sebakhy, Khaled O. / Picchioni, Francesco / van der Wel, Patrick C.A.

    Food hydrocolloids. 2022 June, v. 127

    2022  

    Abstract: Alginate hydrogels are versatile self-assembling biocompatible materials with diverse biomedical and food industrial applications, which includes uses in encapsulation, (drug) delivery and tissue engineering. Hydrogel formation requires cross-linking, ... ...

    Abstract Alginate hydrogels are versatile self-assembling biocompatible materials with diverse biomedical and food industrial applications, which includes uses in encapsulation, (drug) delivery and tissue engineering. Hydrogel formation requires cross-linking, which for alginates is often done with calcium ions that engage in specific interactions with the polysaccharide carboxylic acid groups. Water molecules also hydrate these alginate groups and fill macropores within the hydrogels, with implications for both mechanical properties and cargo encapsulation. Understanding these aspects of hydrogels requires the observation and characterization of the hydrogel waters, how they engage the alginate, and fill the macropores. Here we employed solid-state NMR (ssNMR) spectroscopy to detect and study water molecules in re-hydrated alginate hydrogels. ¹H, ²H, and ¹³C magic angle spinning (MAS) NMR and relaxation measurements were combined to observe both water and alginate. Two different water phases were detected that vary upon gradual (re)hydration of the alginate hydrogels. These water pools differ in their chemical shifts and NMR relaxation properties, reflecting hydration waters directly associated with the carbohydrate polymers alongside dynamic waters in the macropores. Thus, the ssNMR detects the water-filled macropore water pools and how they vary upon calcium cross-linking. We also observe how calcium cross-linking selectively immobilizes the α-guluronate monosaccharides, but leaves the β-mannuronate units more flexible and prone to selective re-hydration. Thus, these ssNMR experiments can be used to probe cross-linking and hydration of alginate hydrogels, with implications for our understanding of design parameters that tune their performance in (drug) delivery and other food industrial applications.
    Keywords alginates ; calcium ; carboxylic acids ; crosslinking ; drugs ; encapsulation ; hydrocolloids ; hydrogels ; macropores ; nuclear magnetic resonance spectroscopy
    Language English
    Dates of publication 2022-06
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 742742-6
    ISSN 1873-7137 ; 0268-005X
    ISSN (online) 1873-7137
    ISSN 0268-005X
    DOI 10.1016/j.foodhyd.2022.107500
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  7. Article ; Online: New insights in polydopamine formation via surface adsorption.

    Hemmatpour, Hamoon / De Luca, Oreste / Crestani, Dominic / Stuart, Marc C A / Lasorsa, Alessia / van der Wel, Patrick C A / Loos, Katja / Giousis, Theodosis / Haddadi-Asl, Vahid / Rudolf, Petra

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 664

    Abstract: Polydopamine is a biomimetic self-adherent polymer, which can be easily deposited on a wide variety of materials. Despite the rapidly increasing interest in polydopamine-based coatings, the polymerization mechanism and the key intermediate species formed ...

    Abstract Polydopamine is a biomimetic self-adherent polymer, which can be easily deposited on a wide variety of materials. Despite the rapidly increasing interest in polydopamine-based coatings, the polymerization mechanism and the key intermediate species formed during the deposition process are still controversial. Herein, we report a systematic investigation of polydopamine formation on halloysite nanotubes; the negative charge and high surface area of halloysite nanotubes favour the capture of intermediates that are involved in polydopamine formation and decelerate the kinetics of the process, to unravel the various polymerization steps. Data from X-ray photoelectron and solid-state nuclear magnetic resonance spectroscopies demonstrate that in the initial stage of polydopamine deposition, oxidative coupling reaction of the dopaminechrome molecules is the main reaction pathway that leads to formation of polycatecholamine oligomers as an intermediate and the post cyclization of the linear oligomers occurs subsequently. Furthermore, TRIS molecules are incorporated into the initially formed oligomers.
    Language English
    Publishing date 2023-02-07
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-36303-8
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  8. Article ; Online: Conformation and Affinity Modulations by Multiple Phosphorylation Occurring in the BIN1 SH3 Domain Binding Site of the Tau Protein Proline-Rich Region.

    Lasorsa, Alessia / Bera, Krishnendu / Malki, Idir / Dupré, Elian / Cantrelle, François-Xavier / Merzougui, Hamida / Sinnaeve, Davy / Hanoulle, Xavier / Hritz, Jozef / Landrieu, Isabelle

    Biochemistry

    2023  Volume 62, Issue 11, Page(s) 1631–1642

    Abstract: An increase in phosphorylation of the Tau protein is associated with Alzheimer's disease (AD) progression through unclear molecular mechanisms. In general, phosphorylation modifies the interaction of intrinsically disordered proteins, such as Tau, with ... ...

    Abstract An increase in phosphorylation of the Tau protein is associated with Alzheimer's disease (AD) progression through unclear molecular mechanisms. In general, phosphorylation modifies the interaction of intrinsically disordered proteins, such as Tau, with other proteins; however, elucidating the structural basis of this regulation mechanism remains challenging. The bridging integrator-1 gene is an AD genetic determinant whose gene product, BIN1, directly interacts with Tau. The proline-rich motif recognized within a Tau(210-240) peptide by the SH3 domain of BIN1 (BIN1 SH3) is defined as
    MeSH term(s) Humans ; tau Proteins/metabolism ; Phosphorylation ; src Homology Domains ; Protein Binding ; Alzheimer Disease/metabolism ; Peptides/chemistry ; Binding Sites ; Proline/metabolism ; Nuclear Proteins/metabolism ; Tumor Suppressor Proteins/chemistry ; Adaptor Proteins, Signal Transducing/metabolism
    Chemical Substances tau Proteins ; Peptides ; Proline (9DLQ4CIU6V) ; BIN1 protein, human ; Nuclear Proteins ; Tumor Suppressor Proteins ; Adaptor Proteins, Signal Transducing
    Language English
    Publishing date 2023-05-11
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.2c00717
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    Zs.A 217: Show issues Location:
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  9. Article ; Online: Interaction of Copper Trafficking Proteins with the Platinum Anticancer Drug Kiteplatin.

    Barbanente, Alessandra / Galliani, Angela / Iacobazzi, Rosa Maria / Lasorsa, Alessia / Nardella, Maria Incoronata / Pennetta, Antonio / Margiotta, Nicola / Arnesano, Fabio

    ChemMedChem

    2021  Volume 17, Issue 1, Page(s) e202100593

    Abstract: The interaction of metallodrugs with proteins influences their mechanism of action and side effects. In the case of platinum drugs, copper transporters modulate sensitivity and resistance to these anticancer agents. To deepen the knowledge of the ... ...

    Abstract The interaction of metallodrugs with proteins influences their mechanism of action and side effects. In the case of platinum drugs, copper transporters modulate sensitivity and resistance to these anticancer agents. To deepen the knowledge of the structural properties underlying the reactivity of platinum drugs with copper transporters, we studied the interaction of kiteplatin and two of its derivatives with the methionine-rich motif of copper importer Ctr1 and with the dithiol motif of the first domain of Menkes ATPase. Furthermore, cellular uptake and cytotoxicity of the three complexes were evaluated in cisplatin-sensitive and -resistant ovarian cancer cells, comparing the data with those of clinically relevant drugs. Reactivity depends on the tightness of the chelate ring formed by the carrier ligands and the nature of the leaving and entering groups. The results highlight the importance of subtle changes in the platinum coordination sphere that affect drug absorption and intracellular fate.
    MeSH term(s) Antineoplastic Agents/chemical synthesis ; Antineoplastic Agents/chemistry ; Antineoplastic Agents/pharmacology ; Cell Line, Tumor ; Cell Proliferation/drug effects ; Cell Survival/drug effects ; Copper Transporter 1/antagonists & inhibitors ; Copper Transporter 1/metabolism ; Dose-Response Relationship, Drug ; Drug Screening Assays, Antitumor ; Humans ; Molecular Structure ; Organoplatinum Compounds/chemical synthesis ; Organoplatinum Compounds/chemistry ; Organoplatinum Compounds/pharmacology ; Structure-Activity Relationship
    Chemical Substances Antineoplastic Agents ; Copper Transporter 1 ; Organoplatinum Compounds ; SLC31A1 protein, human ; platinum(II)(1,4-diazacycloheptane)dichloride
    Language English
    Publishing date 2021-11-15
    Publishing country Germany
    Document type Journal Article ; 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.202100593
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  10. Article: Solid-state NMR spectroscopy insights for resolving different water pools in alginate hydrogels

    El Hariri El Nokab, Mustapha / Lasorsa, Alessia / Sebakhy, Khaled O. / Picchioni, Francesco / van der Wei, Patrick C. A.

    Food hydrocolloids

    2022  Volume 127, Issue -, Page(s) 107500

    Language English
    Document type Article
    ZDB-ID 742742-6
    ISSN 0268-005X
    Database Current Contents Nutrition, Environment, Agriculture

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