LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 73

Search options

  1. Article ; Online: Photoresponsive peptide materials: Spatiotemporal control of self-assembly and biological functions.

    Matsuura, Kazunori / Inaba, Hiroshi

    Biophysics reviews

    2023  Volume 4, Issue 4, Page(s) 41303

    Abstract: Peptides work as both functional molecules to modulate various biological phenomena and self-assembling artificial materials. The introduction of photoresponsive units to peptides allows the spatiotemporal remote control of their structure and function ... ...

    Abstract Peptides work as both functional molecules to modulate various biological phenomena and self-assembling artificial materials. The introduction of photoresponsive units to peptides allows the spatiotemporal remote control of their structure and function upon light irradiation. This article overviews the photoresponsive peptide design, interaction with biomolecules, and applications in self-assembling materials over the last 30 years. Peptides modified with photochromic (photoisomerizable) molecules, such as azobenzene and spiropyran, reversibly photo-controlled the binding to biomolecules and nanostructure formation through self-assembly. Photocleavable molecular units irreversibly control the functions of peptides through cleavage of the main chain and deprotection by light. Photocrosslinking between peptides or between peptides and other biomolecules enhances the structural stability of peptide assemblies and complexes. These photoresponsive peptides spatiotemporally controlled the formation and dissociation of peptide assemblies, gene expressions, protein-drug interactions, protein-protein interactions, liposome deformation and motility, cytoskeleton structure and stability, and cell functions by appropriate light irradiation. These molecular systems can be applied to photo-control biological functions, molecular robots, artificial cells, and next-generation smart drug delivery materials.
    Language English
    Publishing date 2023-12-18
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 2688-4089
    ISSN (online) 2688-4089
    DOI 10.1063/5.0179171
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  2. Article ; Online: Strategy toward In-Cell Self-Assembly of an Artificial Viral Capsid from a Fluorescent Protein-Modified β-Annulus Peptide.

    Sakamoto, Kentarou / Yamamoto, Yuka / Inaba, Hiroshi / Matsuura, Kazunori

    ACS synthetic biology

    2024  

    Abstract: In-cell self-assembly of natural viral capsids is an event that can be visualized under transmission electron microscopy (TEM) observations. By mimicking the self-assembly of natural viral capsids, various artificial protein- and peptide-based nanocages ... ...

    Abstract In-cell self-assembly of natural viral capsids is an event that can be visualized under transmission electron microscopy (TEM) observations. By mimicking the self-assembly of natural viral capsids, various artificial protein- and peptide-based nanocages were developed; however, few studies have reported the in-cell self-assembly of such nanocages. Our group developed a β-Annulus peptide that can form a nanocage called artificial viral capsid in vitro, but in-cell self-assembly of the capsid has not been achieved. Here, we designed an artificial viral capsid decorated with a fluorescent protein, StayGold, to visualize in-cell self-assembly. Fluorescence anisotropy measurements and fluorescence resonance energy transfer imaging, in addition to TEM observations of the cells and super-resolution microscopy, revealed that StayGold-conjugated β-Annulus peptides self-assembled into the StayGold-decorated artificial viral capsid in a cell. Using these techniques, we achieved the in-cell self-assembly of an artificial viral capsid.
    Language English
    Publishing date 2024-05-10
    Publishing country United States
    Document type Journal Article
    ISSN 2161-5063
    ISSN (online) 2161-5063
    DOI 10.1021/acssynbio.4c00135
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  3. Article ; Online: Synthetic approaches to construct viral capsid-like spherical nanomaterials.

    Matsuura, Kazunori

    Chemical communications (Cambridge, England)

    2018  Volume 54, Issue 65, Page(s) 8944–8959

    Abstract: This feature article describes recent progress in synthetic strategies to construct viral capsid-like spherical nanomaterials using the self-assembly of peptides and/or proteins. By mimicking the self-assembly of spherical viral capsids and clathrin, ... ...

    Abstract This feature article describes recent progress in synthetic strategies to construct viral capsid-like spherical nanomaterials using the self-assembly of peptides and/or proteins. By mimicking the self-assembly of spherical viral capsids and clathrin, trigonal peptide conjugates bearing β-sheet-forming peptides, glutathiones, or coiled-coil-forming peptides were developed to construct viral capsid-like particles. β-Annulus peptides from tomato bushy stunt virus self-assembled into viral capsid-like nanocapsules with a size of 30-50 nm, which could encapsulate various guest molecules and be decorated with different molecules on their surface. Rationally designed fusion proteins bearing symmetric assembling units afforded precise viral capsid-like polyhedral assemblies. These synthetic approaches to construct artificial viruses could become useful guidelines to develop novel drug carriers, vaccine platforms, nanotemplates and nanoreactors.
    MeSH term(s) Biomimetic Materials/chemical synthesis ; Biomimetic Materials/chemistry ; Capsid/chemistry ; Drug Carriers/chemical synthesis ; Drug Carriers/chemistry ; HeLa Cells ; Humans ; Macromolecular Substances/chemical synthesis ; Macromolecular Substances/chemistry ; Nanocapsules/chemistry ; Peptides/chemistry ; Proteins/chemistry ; Tombusvirus/chemistry
    Chemical Substances Drug Carriers ; Macromolecular Substances ; Nanocapsules ; Peptides ; Proteins
    Language English
    Publishing date 2018-06-05
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/c8cc03844a
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article ; Online: Encapsulation of Nanomaterials Inside Microtubules by Using a Tau-Derived Peptide.

    Inaba, Hiroshi / Matsuura, Kazunori

    Methods in molecular biology (Clifton, N.J.)

    2022  Volume 2430, Page(s) 243–260

    Abstract: Microtubules (MTs) are tubular cytoskeletons, which are used for the various applications such as active matters and therapeutic targets. Although modification of the exterior surface of MTs is frequently used for functionalization of MTs, there was no ... ...

    Abstract Microtubules (MTs) are tubular cytoskeletons, which are used for the various applications such as active matters and therapeutic targets. Although modification of the exterior surface of MTs is frequently used for functionalization of MTs, there was no approach to introduce molecules inside MTs. We previously developed a unique peptide binding to the inner surface of MT, which is derived from a MT-associated protein, Tau. The Tau-derived peptide (TP) can be used to introduce various nanomaterials inside MTs. Here we describe the TP-based encapsulation of fluorescent dye, gold nanoparticle, green fluorescent protein, and magnetic CoPt nanoparticles inside MTs.
    MeSH term(s) Gold/analysis ; Metal Nanoparticles ; Microtubules/metabolism ; Nanostructures ; Peptides/chemistry ; tau Proteins/metabolism
    Chemical Substances Peptides ; tau Proteins ; Gold (7440-57-5)
    Language English
    Publishing date 2022-04-27
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-1983-4_16
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  5. Article ; Online: A supramolecular system mimicking the infection process of an enveloped virus through membrane fusion.

    Furukawa, Hiroto / Kimura, Yuuna / Inaba, Hiroshi / Matsuura, Kazunori

    Scientific reports

    2023  Volume 13, Issue 1, Page(s) 19934

    Abstract: Membrane fusion is an essential step for the entry of enveloped viruses, such as human immunodeficiency virus and influenza virus, into the host cell, often triggered by the binding of membrane proteins on the viral envelope to host cell membrane. ... ...

    Abstract Membrane fusion is an essential step for the entry of enveloped viruses, such as human immunodeficiency virus and influenza virus, into the host cell, often triggered by the binding of membrane proteins on the viral envelope to host cell membrane. Recently, external stimuli was shown to trigger membrane fusion in an artificial system. Direct observation of artificial membrane fusion using a giant unilamellar vesicle (GUV), which is similar in size to a cell, is useful as a biological model system. However, there are no model systems for studying membrane fusion of enveloped viruses with host cells. Here, we report a supramolecular model system for viral entry into a GUV or cell through membrane fusion. The system was constructed by complexing a cationic lipid bilayer on an anionic artificial viral capsid, self-assembled from viral β-annulus peptides. We demonstrate that the cationic enveloped artificial viral capsid electrostatically interacts with the anionic GUV or cell, and the capsid enters the GUV or cell through membrane fusion. The model system established in this study will be important for analyzing membrane fusion during infection of a natural virus.
    MeSH term(s) Humans ; Membrane Fusion ; Viruses/metabolism ; Virus Internalization ; Peptides/metabolism ; Capsid Proteins/metabolism
    Chemical Substances Peptides ; Capsid Proteins
    Language English
    Publishing date 2023-11-15
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-023-47347-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  6. Article: Dramatic morphological changes in liposomes induced by peptide nanofibers reversibly polymerized and depolymerized by the photoisomerization of spiropyran.

    Liang, Yingbing / Ogawa, Shigesaburo / Inaba, Hiroshi / Matsuura, Kazunori

    Frontiers in molecular biosciences

    2023  Volume 10, Page(s) 1137885

    Abstract: Cytoskeletons such as microtubules and actin filaments are natural protein assemblies, which dynamically control cellular morphology by reversible polymerization/depolymerization. Recently, the control of polymerization/depolymerization of fibrous ... ...

    Abstract Cytoskeletons such as microtubules and actin filaments are natural protein assemblies, which dynamically control cellular morphology by reversible polymerization/depolymerization. Recently, the control of polymerization/depolymerization of fibrous protein/peptide assemblies by external stimuli has attracted significant attention. However, as far as we know, the creation of an "artificial cytoskeleton" that reversibly controls the polymerization/depolymerization of peptide nanofiber in giant unilamellar vesicles (GUVs) has not been reported. Here, we developed peptide nanofiber self-assembled from spiropyran (SP)-modified
    Language English
    Publishing date 2023-03-30
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2814330-9
    ISSN 2296-889X
    ISSN 2296-889X
    DOI 10.3389/fmolb.2023.1137885
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article ; Online: A Photoresponsive Artificial Viral Capsid Self-Assembled from an Azobenzene-Containing

    Matsuura, Kazunori / Fujita, Seiya

    International journal of molecular sciences

    2021  Volume 22, Issue 8

    Abstract: Photoinduced structural changes in peptides can dynamically control the formation and dissociation of supramolecular peptide materials. However, the existence of photoresponsive viral capsids in nature remains unknown. In this study, we constructed an ... ...

    Abstract Photoinduced structural changes in peptides can dynamically control the formation and dissociation of supramolecular peptide materials. However, the existence of photoresponsive viral capsids in nature remains unknown. In this study, we constructed an artificial viral capsid possessing a photochromic azobenzene moiety on the peptide backbone. An azobenzene-containing
    MeSH term(s) Amino Acid Sequence ; Azo Compounds/chemistry ; Capsid/chemistry ; Dynamic Light Scattering ; Isomerism ; Light ; Peptides/chemistry ; Solid-Phase Synthesis Techniques ; Spectrophotometry, Ultraviolet ; Time Factors
    Chemical Substances Azo Compounds ; Peptides ; azobenzene (F0U1H6UG5C)
    Language English
    Publishing date 2021-04-14
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms22084028
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  8. Article ; Online: Live-Cell Fluorescence Imaging of Microtubules by Using a Tau-Derived Peptide.

    Inaba, Hiroshi / Matsuura, Kazunori

    Methods in molecular biology (Clifton, N.J.)

    2021  Volume 2274, Page(s) 169–179

    Abstract: Microtubules (MTs) are important targets for imaging in living cells because of their vital roles in cellular processes. The dynamics (polymerization/depolymerization) of MTs has been imaged in living cells by utilizing MT-targeted drugs as scaffolds. We ...

    Abstract Microtubules (MTs) are important targets for imaging in living cells because of their vital roles in cellular processes. The dynamics (polymerization/depolymerization) of MTs has been imaged in living cells by utilizing MT-targeted drugs as scaffolds. We previously developed a unique MT-binding motif derived from a MT-associated protein, Tau. The Tau-derived peptide (TP) binds to the inner surface of MTs without inhibiting the dynamics of MTs. We introduce a new protocol for live-cell imaging of MTs by using fluorescently labeled TP. We exemplify that tetramethylrhodamine (TMR)-labeled TP (TP-TMR) is spontaneously internalized into HepG2 cells and binds to intracellular MTs, enabling visualization of MTs in living cells. TP-TMR shows no apparent effects on polymerization/depolymerization of MTs and no cytotoxicity. Thus, the peptide-based approach is useful for long-term imaging of MTs.
    MeSH term(s) Cell Survival ; Fluorescence ; Hep G2 Cells ; Humans ; Microtubules/metabolism ; Optical Imaging/methods ; Peptide Fragments/chemistry ; Peptide Fragments/metabolism ; Rhodamines/chemistry ; tau Proteins/metabolism
    Chemical Substances Peptide Fragments ; Rhodamines ; tau Proteins ; tetramethylrhodamine (62669-72-1)
    Language English
    Publishing date 2021-05-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-1258-3_15
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  9. Article: Synthetic approaches to construct viral capsid-like spherical nanomaterials

    Matsuura, Kazunori

    Chemical communications. 2018 Aug. 9, v. 54, no. 65

    2018  

    Abstract: This feature article describes recent progress in synthetic strategies to construct viral capsid-like spherical nanomaterials using the self-assembly of peptides and/or proteins. By mimicking the self-assembly of spherical viral capsids and clathrin, ... ...

    Abstract This feature article describes recent progress in synthetic strategies to construct viral capsid-like spherical nanomaterials using the self-assembly of peptides and/or proteins. By mimicking the self-assembly of spherical viral capsids and clathrin, trigonal peptide conjugates bearing β-sheet-forming peptides, glutathiones, or coiled-coil-forming peptides were developed to construct viral capsid-like particles. β-Annulus peptides from tomato bushy stunt virus self-assembled into viral capsid-like nanocapsules with a size of 30–50 nm, which could encapsulate various guest molecules and be decorated with different molecules on their surface. Rationally designed fusion proteins bearing symmetric assembling units afforded precise viral capsid-like polyhedral assemblies. These synthetic approaches to construct artificial viruses could become useful guidelines to develop novel drug carriers, vaccine platforms, nanotemplates and nanoreactors.
    Keywords capsid ; chemical compounds ; chemical reactions ; clathrin ; drug carriers ; guidelines ; nanocapsules ; peptides ; synthesis ; Tomato bushy stunt virus ; vaccines ; viruses
    Language English
    Dates of publication 2018-0809
    Size p. 8944-8959.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/c8cc03844a
    Database NAL-Catalogue (AGRICOLA)

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  10. Article ; Online: An artificial viral capsid decorated with a DNA aptamer internalizing into lymphoma cells.

    Sakamoto, Kentarou / Uchiyama, Kohsuke / Iwasaki, Takashi / Inaba, Hiroshi / Matsuura, Kazunori

    Journal of materials chemistry. B

    2023  Volume 11, Issue 26, Page(s) 6053–6059

    Abstract: Tumor-specific drug-delivering nanocarriers could be a promising modality for next-generation tumor therapy. Here we developed a Burkitt lymphoma-specific DNA aptamer-labeled nanocarrier using the β-Annulus peptide, which forms a spherical nanoassembly ... ...

    Abstract Tumor-specific drug-delivering nanocarriers could be a promising modality for next-generation tumor therapy. Here we developed a Burkitt lymphoma-specific DNA aptamer-labeled nanocarrier using the β-Annulus peptide, which forms a spherical nanoassembly called artificial viral capsid. Dynamic light scattering and transmission electron microscopy of the DNA aptamer-decorated artificial viral capsid showed the formation of spherical assemblies with a diameter of approximately 50-150 nm. The artificial viral capsid was selectively internalized into the Burkitt lymphoma cell line, Daudi, and doxorubicin complexed with the capsid selectively killed Daudi cells.
    MeSH term(s) Humans ; Aptamers, Nucleotide ; Capsid ; Burkitt Lymphoma/drug therapy ; Peptides ; Doxorubicin/pharmacology
    Chemical Substances Aptamers, Nucleotide ; Peptides ; Doxorubicin (80168379AG)
    Language English
    Publishing date 2023-07-05
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2702241-9
    ISSN 2050-7518 ; 2050-750X
    ISSN (online) 2050-7518
    ISSN 2050-750X
    DOI 10.1039/d3tb00169e
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top