6 research outputs found

    Multiplexing Natural Orientation: Oppositely Directed Self-Assembling Peptides

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    We explore here the possibility that polypeptide chains with directional multiplicity might provide for the control of peptide self-assembly processes. We tested this new possibility using an oppositely directed peptide (ODP) supramolecular system. The ODP could make it possible to form a βαβ motif with antiparallel β-sheets, which does not exist in nature. Furthermore, the designed ODPs were able to self-assemble into discrete, homogeneous, and structured protein-like controlled nano-objects. ODPs represent a simple but powerful unnatural self-assembling peptide system that can become a basic scaffold for fabricating more complex and elaborate artificial nanostructures

    Structural and Conformational Dynamics of Self-Assembling Bioactive β‑Sheet Peptide Nanostructures Decorated with Multivalent RNA-Binding Peptides

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    Understanding the dynamic behavior of nanostructural systems is important during the development of controllable and tailor-made nanomaterials. This is particularly true for nanostructures that are intended for biological applications because biomolecules are usually highly dynamic and responsive to external stimuli. In this Article, we investigated the structural and conformational dynamics of self-assembling bioactive β-sheet peptide nanostructures using electron paramagnetic resonance (EPR) spectroscopy. The model peptide nanostructures are characterized by the cross-β spine of β-ribbon fibers and multiple RNA-binding bioactive peptides that constitute the shell of the nanostructures. We found first, that bioactive peptides at the shell of β-ribbon nanostructure have a mobility similar to that of an isolated monomeric peptide. Second, the periphery of the cross-β spine is more immobile than the distal part of surface-displayed bioactive peptides. Third, the rotational dynamics of short and long fibrils are similar; that is, the mobility is largely independent of the extent of aggregation. Fourth, peptides that constitute the shell are affected first by the external environment at the initial stage. The cross-β spine resists its external environment to a certain extent and abruptly disintegrates when the perturbation reaches a certain degree. Our results provide an overall picture of β-sheet peptide nanostructure dynamics, which should be useful in the development of dynamic self-assembled peptide nanostructures

    Nanomorphological Diversity of Self-Assembled Cyclopeptisomes Investigated via Thermodynamic and Kinetic Controls

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    The physicochemical and biological characteristics of vesicles are dependent on the type of self-assembly building blocks and methods of preparation. In this report, we designed a vesicle-forming linear and cyclic peptide building blocks and investigated the effect of molecular topology and thermodynamic and kinetic controls on the stability and morphological features of the self-assembled vesicles. Comparison of topological effect on self-assembly revealed that the strong association of the aromatic hydrophobic segments is observed only in the cyclic peptide, which is most likely the results of constrained structure along with the restriction in the molecular degree of freedom. Consequently, the formation of stable vesicles could be observed only with the cyclic peptide. Further investigation with cyclic peptide building blocks revealed that depending on the control methods, vesicles with a variety of structural features, such as polygonal, wrinkled, round, round-patched, and round-fused vesicles, could be fabricated. Our results demonstrate that existing vesicle structures constitute only a fraction of the possible structural diversity and that macrocyclic peptides can provide a wealth of opportunities in vesicle engineering

    Additional file 1 of Association between decreased ipsilateral renal function and aggressive behavior in renal cell carcinoma

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    Additional file 1: Supplementary Table 1. Comparison of characteristics between maintained and decreased ipsilateral SRF in synchronous metastatic renal cell carcinoma
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