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  1. Article ; Online: Self-assembly of coiled coils in synthetic biology: inspiration and progress.

    Robson Marsden, Hana / Kros, Alexander

    Angewandte Chemie (International ed. in English)

    2010  Volume 49, Issue 17, Page(s) 2988–3005

    Abstract: Biological self-assembly is very complex and results in highly functional materials. In effect, it takes a bottom-up approach using biomolecular building blocks of precisely defined shape, size, hydrophobicity, and spatial distribution of functionality. ... ...

    Abstract Biological self-assembly is very complex and results in highly functional materials. In effect, it takes a bottom-up approach using biomolecular building blocks of precisely defined shape, size, hydrophobicity, and spatial distribution of functionality. Inspired by, and drawing lessons from self-assembly processes in nature, scientists are learning how to control the balance of many small forces to increase the complexity and functionality of self-assembled nanomaterials. The coiled-coil motif, a multipurpose building block commonly found in nature, has great potential in synthetic biology. In this review we examine the roles that the coiled-coil peptide motif plays in self-assembly in nature, and then summarize the advances that this has inspired in the creation of functional units, assemblies, and systems.
    MeSH term(s) Amino Acid Motifs ; Animals ; Biomimetics ; Humans ; Models, Molecular ; Molecular Motor Proteins/chemistry ; Peptides/chemistry
    Chemical Substances Molecular Motor Proteins ; Peptides
    Language English
    Publishing date 2010-04-12
    Publishing country Germany
    Document type Journal Article ; Review
    ZDB-ID 2011836-3
    ISSN 1521-3773 ; 1433-7851
    ISSN (online) 1521-3773
    ISSN 1433-7851
    DOI 10.1002/anie.200904943
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Polymer-peptide block copolymers - an overview and assessment of synthesis methods.

    Robson Marsden, Hana / Kros, Alexander

    Macromolecular bioscience

    2009  Volume 9, Issue 10, Page(s) 939–951

    Abstract: Incorporating peptide blocks into block copolymers opens up new realms of bioactive or smart materials. Because there are such a variety of peptides, polymers, and hybrid architectures that can be imagined, there are many different routes available for ... ...

    Abstract Incorporating peptide blocks into block copolymers opens up new realms of bioactive or smart materials. Because there are such a variety of peptides, polymers, and hybrid architectures that can be imagined, there are many different routes available for the synthesis of these chimera molecules. This review summarizes the contemporary strategies in combining synthesis techniques to create well-defined peptide-polymer hybrids that retain the vital aspects of each disparate block. Living polymerization can be united with the molecular-level control afforded by peptide blocks to yield block copolymers that not only have precisely defined primary structures, but that also interact with other (bio)molecules in a well defined manner.
    MeSH term(s) Amino Acid Sequence ; Hydrogen-Ion Concentration ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Peptides/chemical synthesis ; Peptides/chemistry ; Polymers/chemical synthesis ; Polymers/chemistry ; Protein Structure, Secondary ; Solutions/chemistry
    Chemical Substances Peptides ; Polymers ; Solutions
    Language English
    Publishing date 2009-10-08
    Publishing country Germany
    Document type Journal Article ; Review
    ZDB-ID 2039130-4
    ISSN 1616-5195 ; 1616-5187
    ISSN (online) 1616-5195
    ISSN 1616-5187
    DOI 10.1002/mabi.200900057
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Introducing quadrupole interactions into the peptide design toolkit.

    Robson Marsden, Hana / Fraaije, Johannes G E M / Kros, Alexander

    Angewandte Chemie (International ed. in English)

    2010  Volume 49, Issue 46, Page(s) 8570–8572

    MeSH term(s) Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Peptides/chemistry ; Protein Binding ; Quantum Theory ; Static Electricity
    Chemical Substances Peptides
    Language English
    Publishing date 2010-11-08
    Publishing country Germany
    Document type Comment ; Journal Article
    ZDB-ID 2011836-3
    ISSN 1521-3773 ; 1433-7851
    ISSN (online) 1521-3773
    ISSN 1433-7851
    DOI 10.1002/anie.201003828
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Self-Assembly of Coiled Coils in Synthetic Biology: Inspiration and Progress

    Robson Marsden, Hana / Kros, Alexander

    Angewandte Chemie. 2010 Apr. 12, v. 49, no. 17

    2010  

    Abstract: Biological self-assembly is very complex and results in highly functional materials. In effect, it takes a bottom-up approach using biomolecular building blocks of precisely defined shape, size, hydrophobicity, and spatial distribution of functionality. ... ...

    Abstract Biological self-assembly is very complex and results in highly functional materials. In effect, it takes a bottom-up approach using biomolecular building blocks of precisely defined shape, size, hydrophobicity, and spatial distribution of functionality. Inspired by, and drawing lessons from self-assembly processes in nature, scientists are learning how to control the balance of many small forces to increase the complexity and functionality of self-assembled nanomaterials. The coiled-coil motif, a multipurpose building block commonly found in nature, has great potential in synthetic biology. In this review we examine the roles that the coiled-coil peptide motif plays in self-assembly in nature, and then summarize the advances that this has inspired in the creation of functional units, assemblies, and systems.
    Language English
    Dates of publication 2010-0412
    Size p. 2988-3005.
    Publishing place Wiley-VCH Verlag
    Document type Article
    ZDB-ID 2011836-3
    ISSN 1521-3773 ; 1433-7851
    ISSN (online) 1521-3773
    ISSN 1433-7851
    DOI 10.1002/anie.200904943
    Database NAL-Catalogue (AGRICOLA)

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  5. Article ; Online: Model systems for membrane fusion.

    Marsden, Hana Robson / Tomatsu, Itsuro / Kros, Alexander

    Chemical Society reviews

    2011  Volume 40, Issue 3, Page(s) 1572–1585

    Abstract: Membrane fusion has an overarching influence on living organisms. The fusion of sperm and egg membranes initiates the life of a sexually reproducing organism. Intracellular membrane fusion facilitates molecular trafficking within every cell of the ... ...

    Abstract Membrane fusion has an overarching influence on living organisms. The fusion of sperm and egg membranes initiates the life of a sexually reproducing organism. Intracellular membrane fusion facilitates molecular trafficking within every cell of the organism during its entire lifetime, and virus-cell membrane fusion may signal the end of the organism's life. Considering its importance, surprisingly little is known about the molecular-level mechanism of membrane fusion. Due to the complexity of a living cell, observations often leave room for ambiguity in interpretation. Therefore artificial model systems composed of only a few components are being used to further our understanding of controlled fusion processes. In this critical review we first give an overview of the hypothesized mechanism of membrane fusion and the techniques that are used to investigate it, and then present a selection of non-targeted and targeted model systems, finishing with current applications and predictions on future developments (85 references).
    MeSH term(s) Lipid Bilayers/chemistry ; Liposomes/chemistry ; Membrane Fusion ; Models, Molecular ; Nanotechnology ; SNARE Proteins/chemistry
    Chemical Substances Lipid Bilayers ; Liposomes ; SNARE Proteins
    Language English
    Publishing date 2011-03
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1472875-8
    ISSN 1460-4744 ; 0306-0012
    ISSN (online) 1460-4744
    ISSN 0306-0012
    DOI 10.1039/c0cs00115e
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Controlled liposome fusion mediated by SNARE protein mimics

    Robson Marsden, Hana / Korobko, Alexander V / Kros, Alexander / Voskuhl, Jens / Zheng, Tingting

    Biomaterials science. 2013 Aug. 28, v. 1, no. 10

    2013  

    Abstract: The fusion of lipid membranes is essential for the delivery of chemicals across biological barriers to specific cellular locations. Intracellular membrane fusion is particularly precise and is critically mediated by SNARE proteins. To allow membrane ... ...

    Abstract The fusion of lipid membranes is essential for the delivery of chemicals across biological barriers to specific cellular locations. Intracellular membrane fusion is particularly precise and is critically mediated by SNARE proteins. To allow membrane fusion to be better understood and harnessed we have mimicked this important process with a simple bottom-up model in which synthetic fusogens replicate the essential features of SNARE proteins. In our fusogens, the coiled-coil molecular recognition motif of SNARE proteins is replaced by the coiled-coil E/K peptide complex, which is one-ninth the size. The peptides are anchored in liposome membranes via pegylated lipids. Here we discuss how the liposome fusion process is controlled by different parameters within the minimal model. The lipopeptide fusogens form specific coiled coils that dock liposomes together, resulting in the merging of membranes via the stalk intermediate. Unusually for model systems, the lipopeptides can rapidly lead to fusion of entire liposome populations and the liposomes can undergo many rounds of fusion. The rate and extent of fusion and the number of fusion rounds can be manipulated by adjusting the fusogen and liposome concentrations. For example, these parameters can be tuned such that tens of thousands of ∼100 nm liposomes fuse into a single giant liposome ∼10 μm in diameter; alternatively, conditions can be selected such that only two liposomes fuse. The improved understanding of membrane fusion shows how application-specific fusion attributes can be achieved, and paves the way for controlled nanoreactor mixing and controlled delivery of cargo to cells.
    Keywords lipopeptides ; membrane fusion ; mixing ; models ; SNARE proteins
    Language English
    Dates of publication 2013-0828
    Size p. 1046-1054.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ZDB-ID 2693928-9
    ISSN 2047-4849 ; 2047-4830
    ISSN (online) 2047-4849
    ISSN 2047-4830
    DOI 10.1039/c3bm60040h
    Database NAL-Catalogue (AGRICOLA)

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  7. Article: Introducing Quadrupole Interactions into the Peptide Design Toolkit

    Robson Marsden, Hana / Fraaije, Johannes G.E.M / Kros, Alexander

    Angewandte Chemie. 2010 Nov. 8, v. 49, no. 46

    2010  

    Language English
    Dates of publication 2010-1108
    Size p. 8570-8572.
    Publishing place Wiley‐VCH Verlag
    Document type Article
    ZDB-ID 2011836-3
    ISSN 1521-3773 ; 1433-7851
    ISSN (online) 1521-3773
    ISSN 1433-7851
    DOI 10.1002/anie.201003828
    Database NAL-Catalogue (AGRICOLA)

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  8. Article: Model systems for membrane fusion

    Marsden, Hana Robson / Tomatsu, Itsuro / Kros, Alexander

    Chemical Society reviews. 2011 Feb. 22, v. 40, no. 3

    2011  

    Abstract: Membrane fusion has an overarching influence on living organisms. The fusion of sperm and eggmembranes initiates the life of a sexually reproducing organism. Intracellularmembrane fusion facilitates molecular trafficking within every cell of the organism ...

    Abstract Membrane fusion has an overarching influence on living organisms. The fusion of sperm and eggmembranes initiates the life of a sexually reproducing organism. Intracellularmembrane fusion facilitates molecular trafficking within every cell of the organism during its entire lifetime, and virus-cell membrane fusion may signal the end of the organism's life. Considering its importance, surprisingly little is known about the molecular-level mechanism of membrane fusion. Due to the complexity of a living cell, observations often leave room for ambiguity in interpretation. Therefore artificial model systems composed of only a few components are being used to further our understanding of controlled fusion processes. In this critical review we first give an overview of the hypothesized mechanism of membrane fusion and the techniques that are used to investigate it, and then present a selection of non-targeted and targeted model systems, finishing with current applications and predictions on future developments (85 references).
    Keywords finishing ; membrane fusion ; models ; prediction ; sexual reproduction ; spermatozoa
    Language English
    Dates of publication 2011-0222
    Size p. 1572-1585.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ZDB-ID 1472875-8
    ISSN 1460-4744 ; 0306-0012
    ISSN (online) 1460-4744
    ISSN 0306-0012
    DOI 10.1039/c0cs00115e
    Database NAL-Catalogue (AGRICOLA)

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  9. Article ; Online: Controlled liposome fusion mediated by SNARE protein mimics.

    Robson Marsden, Hana / Korobko, Alexander V / Zheng, Tingting / Voskuhl, Jens / Kros, Alexander

    Biomaterials science

    2013  Volume 1, Issue 10, Page(s) 1046–1054

    Abstract: The fusion of lipid membranes is essential for the delivery of chemicals across biological barriers to specific cellular locations. Intracellular membrane fusion is particularly precise and is critically mediated by SNARE proteins. To allow membrane ... ...

    Abstract The fusion of lipid membranes is essential for the delivery of chemicals across biological barriers to specific cellular locations. Intracellular membrane fusion is particularly precise and is critically mediated by SNARE proteins. To allow membrane fusion to be better understood and harnessed we have mimicked this important process with a simple bottom-up model in which synthetic fusogens replicate the essential features of SNARE proteins. In our fusogens, the coiled-coil molecular recognition motif of SNARE proteins is replaced by the coiled-coil E/K peptide complex, which is one-ninth the size. The peptides are anchored in liposome membranes via pegylated lipids. Here we discuss how the liposome fusion process is controlled by different parameters within the minimal model. The lipopeptide fusogens form specific coiled coils that dock liposomes together, resulting in the merging of membranes via the stalk intermediate. Unusually for model systems, the lipopeptides can rapidly lead to fusion of entire liposome populations and the liposomes can undergo many rounds of fusion. The rate and extent of fusion and the number of fusion rounds can be manipulated by adjusting the fusogen and liposome concentrations. For example, these parameters can be tuned such that tens of thousands of ∼100 nm liposomes fuse into a single giant liposome ∼10 μm in diameter; alternatively, conditions can be selected such that only two liposomes fuse. The improved understanding of membrane fusion shows how application-specific fusion attributes can be achieved, and paves the way for controlled nanoreactor mixing and controlled delivery of cargo to cells.
    Language English
    Publishing date 2013-06-04
    Publishing country England
    Document type Journal Article
    ZDB-ID 2693928-9
    ISSN 2047-4849 ; 2047-4830
    ISSN (online) 2047-4849
    ISSN 2047-4830
    DOI 10.1039/c3bm60040h
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Probing coiled-coil assembly by paramagnetic NMR spectroscopy.

    Zheng, TingTing / Boyle, Aimee / Robson Marsden, Hana / Valdink, Dayenne / Martelli, Giuliana / Raap, Jan / Kros, Alexander

    Organic & biomolecular chemistry

    2015  Volume 13, Issue 4, Page(s) 1159–1168

    Abstract: Here a new method to determine the oligomeric state and orientation of coiled-coil peptide motifs is described. Peptides K and E, which are designed to form a parallel heterodimeric complex in aqueous solution, were labeled with the aromatic amino acids ... ...

    Abstract Here a new method to determine the oligomeric state and orientation of coiled-coil peptide motifs is described. Peptides K and E, which are designed to form a parallel heterodimeric complex in aqueous solution, were labeled with the aromatic amino acids tryptophan and tyrosine on the C-terminus respectively as 'fingerprint' residues. One of the peptides was also labeled with the paramagnetic probe MTSL. One dimensional proton NMR spectroscopy was used to study the peptide quaternary structure by monitoring the signal suppression of the aromatic labels due to proximity of the nitroxyl radical. 1D-NMR confirmed that the peptides K and E form a heterodimeric coiled coil with a parallel orientation. In addition, fluorescence emission quenching of the aromatic labels due to electron exchange with a nitroxyl radical confirmed the parallel coiled coil orientation. Thus, paramagnetic nitroxide and aromatic fluorophore labeling of peptides yields valuable information regarding the quaternary structure from 1D-NMR and steady-state fluorescence measurements. This convenient method is useful not only to investigate coiled coil assembly, but can also be applied to any defined supramolecular assembly.
    MeSH term(s) Amino Acid Sequence ; Dimerization ; Magnetic Resonance Spectroscopy/methods ; Molecular Sequence Data ; Nitrogen Oxides/chemistry ; Peptides/chemistry ; Protein Structure, Secondary
    Chemical Substances Nitrogen Oxides ; Peptides ; nitroxyl (GFQ4MMS07W)
    Language English
    Publishing date 2015-01-28
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2097583-1
    ISSN 1477-0539 ; 1477-0520
    ISSN (online) 1477-0539
    ISSN 1477-0520
    DOI 10.1039/c4ob02125h
    Database MEDical Literature Analysis and Retrieval System OnLINE

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