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WIREs Nanomed Nanobiotechnol
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α‐Helical coiled‐coil peptide materials for biomedical applications

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Self‐assembling coiled coils, which occur commonly in native proteins, have received significant interest for the design of new biomaterials‐based medical therapies. Considerable effort over recent years has led to a detailed understanding of the self‐assembly process of coiled coils, and a diverse collection of strategies have been developed for designing functional materials using this motif. The ability to engineer the interface between coiled coils allows one to achieve variously connected components, leading to precisely defined structures such as nanofibers, nanotubes, nanoparticles, networks, gels, and combinations of these. Currently these materials are being developed for a range of biotechnological and medical applications, including drug delivery systems for controlled release, targeted nanomaterials, ‘drug‐free’ therapeutics, vaccine delivery systems, and others. WIREs Nanomed Nanobiotechnol 2017, 9:e1424. doi: 10.1002/wnan.1424 This article is categorized under: Nanotechnology Approaches to Biology > Nanoscale Systems in Biology Biology-Inspired Nanomaterials > Peptide-Based Structures
Peptide‐based nanotubes (PNTs) formed from coiled coils. (a) Ribbon diagrams of coiled‐coil assemblies: tetramers (orange; 3R4A), pentamers (Cyan; 4PN8), hexamers (blue; 3R3K), and heptamers (purple; 4PNA). (b) Schematic of helical barrel assembly into PNT. (c) TEM of PNTs formed from hexamers. (Reprinted with permission from Ref . Copyright 2015 American Chemical Society)
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Coiled‐coil nanotubes based upon peptides inspired by TolC protein, designed by Conticello et al. a) 29‐amino acid peptide sequences in two forms, one having arginines in the positions indicated (Form I) and the other containing lysines in those positions (Form II). CryoTEM image (b) and 3D structure (d) of Form I nanotubes; cryoTEM image (c) and 3D structure (e) of Form II nanotubes. (Reprinted with permission from Ref . Copyright 2006 Elsevier)
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Schematic representation and STEM image of coiled coil ‘lock washer’ nanotubes. (a) Schematic of lock washer self‐assembly using peptides derived from the 7‐helix bundle of 7HSAP1, with negatively charged C‐terminal residues (glutamic acid) in red and positively charged N‐terminal residues (lysine) in blue. (b) STEM image of 7HSAP1 nanotubes formed in MES buffer (10 mM, pH 6.0). (Reprinted with permission from Ref . Copyright 2013 American Chemical Society)
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α‐helical coiled‐coil peptide nanofibers designed by Hartgerink et al. (a) Proposed mechanism of self‐assembly into fibers. (b) Representative cryoTEM image of self‐assembling nanofibers. (Reprinted with permission from Ref . Copyright 2008 American Chemical Society)
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Different morphologies created using the ‘sticky ended’ self‐assembling fiber (SAF) system of Woolfson. (a) TEM images of (left to right) straight, kinked, branched, and segmented coiled coil fibers. (b) Schematic representations of the different assembly models, where red and blue arrows represent sticky ended dimeric coiled‐coil peptides and black arrows represent peptides for introducing structural features into the nanofiber morphology. (Reprinted with permission from Ref . Copyright 2006 Elsevier)
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Helical wheel diagram showing the positions of the (abcdefg) heptad repeat residues in a parallel coiled coil; the arrows indicate the hydrophobic interactions between positions a and d and the electrostatic interactions between positions e and g.
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Schematic illustration of coiled coils used for multivalent antigen display in diagnostics and bioassays. Conjugation of a peptide epitope (Ep01) to coiled‐coil peptide fibers (FF03) produces multivalent platforms with enhanced antibody detection capabilities compared with the monovalent system. (Reprinted with permission from Ref . Copyright 2015 American Chemical Society)
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Schematic of self‐assembling polypeptide nanoparticles (SAPN). (a) Ribbon representation of a building block incorporating a trimeric coiled coil, a pentameric coiled coil, and a trimeric coiled‐coil B cell epitope (HRC1). (b) 3D models of the nanoparticles formed from 60 peptides (top), and 180 peptides (bottom). (Reprinted with permission from Ref . Copyright 2008 Wiley)
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Schematic of ‘drug‐free’ therapeutics using polymer‐coiled coil conjugates. The cell surfaces of human Burkitt′s NHL B cells were decorated with one half of a coiled‐coil binding partner (CCE peptide) by binding a CCE peptide/antiCD20 Fab′ conjugate to cell‐surface CD20. Subsequent binding with HPMA copolymers presenting complementary CCK coils led to cross‐linking of the CD20 receptors and subsequent apoptosis. (Reprinted with permission from Ref . Copyright 2010 Wiley)
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Schematic of different decoration strategies for self‐assembling peptide fibers (SAFs). (a) Peptide fibers are assembled by mixing equal amounts of SAF‐p1 and SAF‐p2a at pH 7.4. (b) Non‐covalent decoration using short peptides (SAF‐tags). Rhodamine was attached to the N‐terminus of the tag and visualized via light microscopy. (c) ‘Click’ chemistry was employed for post‐assembly functionalization of fibers incorporating azide groups. The decoration was carried out by reacting the surface azide moieties with biotin‐alkyne, followed by the addition of 5‐nm streptavidin nanogold. The decorated nanofiber was confirmed with TEM imaging. (Reprinted with permission from Ref . Copyright 2010 The Royal Society of Chemistry)
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Schematic of controlled drug release for a peptide‐lipid hybrid system triggered by hyperthermia (HT), with DOX represented by orange dots. (Reprinted with permission from Ref . Copyright 2012 American Chemical Society)
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Schematic illustration of a polymer/protein delivery complex with peptide E and peptide K as the non‐covalently binding linker. (Reprinted with permission from Ref . Copyright 2011 American Chemical Society)
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Schematic representation of the structure of noncovalent poly(N‐(2‐hydroxypropyl)methacrylamide) (PHPMA)‐based polymer/fluorescent dye complex. Oregon Green is the model cargo for delivery. The subscripts x and y represent the mole fractions of HPMA and peptide methacrylate repeat units in the final copolymers. (Reprinted with permission from Ref . Copyright 2010 American Chemical Society)
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Side view of the RHCC protein tetramer containing Pt(IV) prodrug, where the RHCC protein is shown by van der Waals spheres and ribbon representation, with different colors for each helical chain, and the Pt(IV) prodrugs are represented by red spheres. (Reprinted with permission from Ref . Copyright 2015 Elsevier)
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Single‐chain polypeptide tetrahedron. (a) Schematic representation of the self‐assembled tetrahedron designed by Jerala et al. Design elements contained antiparallel coiled‐coil homodimers (1–3, 3, 4, 4, 5, 5–11), parallel heterodimers (2–6, 6, 7, 7, 8, 8, 9, 9, 10, 10–12), and a parallel homodimer (4–7). (b) TEM images and three‐dimensional projections of tetrahedra with different orientations, with uranyl acetate staining of the vertices. (Reprinted with permission from Ref . Copyright 2013 Macmillan Publishers Ltd)
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Self‐assembling cages from coiled‐coil peptides. (a) The design scheme of self‐assembling cages. Homotrimeric coiled coils (CC‐Tri3, green) and dimeric coiled coils (CC‐Di‐A, red; CC‐Di‐B, blue) from Hub A and Hub B by covalently conjugating CC‐Tri3 with CC‐Di‐A and CC‐Di‐B, respectively. Mixing Hub A and Hub B yielded a hexagonal network, while combining Hub A with CC‐Di‐B or combining Hub B with CC‐Di‐A yields discrete structures. (b) SEM images of cages assembled in PBS. (c) Three‐dimensional representation of a single cage as measured by AFM. (Reprinted with permission from Ref . Copyright 2013 American Association for the Advancement of Science)
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Nanotechnology Approaches to Biology > Nanoscale Systems in Biology
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