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Article ; Online: Structures of synthetic helical filaments and tubes based on peptide and peptido-mimetic polymers.

Miller, Jessalyn G / Hughes, Spencer A / Modlin, Charles / Conticello, Vincent P

2022 , Page(s) 1–103

Language	English
Publishing date	2022-03-21
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	209912-3
ISSN	1469-8994 ; 0033-5835
ISSN (online)	1469-8994
ISSN	0033-5835
DOI	10.1017/S0033583522000014
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Article: Cryo-EM of Helical Polymers

Wang, Fengbin / Gnewou, Ordy / Solemanifar, Armin / Conticello, Vincent P. / Egelman, Edward H.

Chemical reviews. 2022 Feb. 08, v. 122, no. 17

2022

Abstract: While the application of cryogenic electron microscopy (cryo-EM) to helical polymers in biology has a long history, due to the huge number of helical macromolecular assemblies in viruses, bacteria, archaea, and eukaryotes, the use of cryo-EM to study ... ...

Abstract	While the application of cryogenic electron microscopy (cryo-EM) to helical polymers in biology has a long history, due to the huge number of helical macromolecular assemblies in viruses, bacteria, archaea, and eukaryotes, the use of cryo-EM to study synthetic soft matter noncovalent polymers has been much more limited. This has mainly been due to the lack of familiarity with cryo-EM in the materials science and chemistry communities, in contrast to the fact that cryo-EM was developed as a biological technique. Nevertheless, the relatively few structures of self-assembled peptide nanotubes and ribbons solved at near-atomic resolution by cryo-EM have demonstrated that cryo-EM should be the method of choice for a structural analysis of synthetic helical filaments. In addition, cryo-EM has also demonstrated that the self-assembly of soft matter polymers has enormous potential for polymorphism, something that may be obscured by techniques such as scattering and spectroscopy. These cryo-EM structures have revealed how far we currently are from being able to predict the structure of these polymers due to their chaotic self-assembly behavior.
Keywords	Archaea ; chemistry ; electron microscopy ; eukaryotic cells ; nanotubes ; peptides ; spectroscopy
Language	English
Dates of publication	2022-0208
Size	p. 14055-14065.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	207949-5
ISSN	1520-6890 ; 0009-2665
ISSN (online)	1520-6890
ISSN	0009-2665
DOI	10.1021/acs.chemrev.1c00753
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Article ; Online: Programmable Fabrication of Multilayer Collagen Nanosheets of Defined Composition.

Jiang, Tao / Conticello, Vincent P

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

2018 Volume 1777, Page(s) 221–232

Abstract: Two-dimensional nanostructures offer significant promise as components for the construction of functional biomaterials. However, the controllable fabrication of these structures remains a challenge. Ideally, one desires to control the composition, ... ...

Abstract	Two-dimensional nanostructures offer significant promise as components for the construction of functional biomaterials. However, the controllable fabrication of these structures remains a challenge. Ideally, one desires to control the composition, structure, and surface functionality of the resultant materials with precision, in order to tailor properties for a particular application and minimize the unintended side effects. We recently reported the synthesis of triple-layer nanosheets from template-driven assembly of a negatively charged collagen-mimetic peptide CP
MeSH term(s)	Chromatography, High Pressure Liquid ; Circular Dichroism ; Collagen/chemistry ; Nanostructures/chemistry ; Nanostructures/ultrastructure ; Peptides/chemical synthesis ; Peptides/chemistry ; Peptides/isolation & purification ; Protein Multimerization ; Proteolysis ; Solid-Phase Synthesis Techniques ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Chemical Substances	Peptides ; Collagen (9007-34-5)
Language	English
Publishing date	2018-05-09
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-7811-3_13
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Article ; Online: Cryo-EM of Helical Polymers.

Wang, Fengbin / Gnewou, Ordy / Solemanifar, Armin / Conticello, Vincent P / Egelman, Edward H

Chemical reviews

2022 Volume 122, Issue 17, Page(s) 14055–14065

Abstract	While the application of cryogenic electron microscopy (cryo-EM) to helical polymers in biology has a long history, due to the huge number of helical macromolecular assemblies in viruses, bacteria, archaea, and eukaryotes, the use of cryo-EM to study synthetic soft matter noncovalent polymers has been much more limited. This has mainly been due to the lack of familiarity with cryo-EM in the materials science and chemistry communities, in contrast to the fact that cryo-EM was developed as a biological technique. Nevertheless, the relatively few structures of self-assembled peptide nanotubes and ribbons solved at near-atomic resolution by cryo-EM have demonstrated that cryo-EM should be the method of choice for a structural analysis of synthetic helical filaments. In addition, cryo-EM has also demonstrated that the self-assembly of soft matter polymers has enormous potential for polymorphism, something that may be obscured by techniques such as scattering and spectroscopy. These cryo-EM structures have revealed how far we currently are from being able to predict the structure of these polymers due to their chaotic self-assembly behavior.
MeSH term(s)	Cryoelectron Microscopy/methods ; Macromolecular Substances ; Polymers ; Viruses/chemistry
Chemical Substances	Macromolecular Substances ; Polymers
Language	English
Publishing date	2022-02-08
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	207949-5
ISSN	1520-6890 ; 0009-2665
ISSN (online)	1520-6890
ISSN	0009-2665
DOI	10.1021/acs.chemrev.1c00753
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Article ; Online: Phenol-soluble modulins PSMα3 and PSMβ2 form nanotubes that are cross-α amyloids.

Kreutzberger, Mark A B / Wang, Shengyuan / Beltran, Leticia C / Tuachi, Abraham / Zuo, Xiaobing / Egelman, Edward H / Conticello, Vincent P

Proceedings of the National Academy of Sciences of the United States of America

2022 Volume 119, Issue 20, Page(s) e2121586119

Abstract: Phenol-soluble modulins (PSMs) are peptide-based virulence factors that play significant roles in the pathogenesis of staphylococcal strains in community-associated and hospital-associated infections. In addition to cytotoxicity, PSMs display the ... ...

Abstract	Phenol-soluble modulins (PSMs) are peptide-based virulence factors that play significant roles in the pathogenesis of staphylococcal strains in community-associated and hospital-associated infections. In addition to cytotoxicity, PSMs display the propensity to self-assemble into fibrillar species, which may be mediated through the formation of amphipathic conformations. Here, we analyze the self-assembly behavior of two PSMs, PSMα3 and PSMβ2, which are derived from peptides expressed by methicillin-resistant Staphylococcus aureus (MRSA), a significant human pathogen. In both cases, we observed the formation of a mixture of self-assembled species including twisted filaments, helical ribbons, and nanotubes, which can reversibly interconvert in vitro. Cryo–electron microscopy structural analysis of three PSM nanotubes, two derived from PSMα3 and one from PSMβ2, revealed that the assemblies displayed remarkably similar structures based on lateral association of cross-α amyloid protofilaments. The amphipathic helical conformations of PSMα3 and PSMβ2 enforced a bilayer arrangement within the protofilaments that defined the structures of the respective PSMα3 and PSMβ2 nanotubes. We demonstrate that, similar to amyloids based on cross-β protofilaments, cross-α amyloids derived from these PSMs display polymorphism, not only in terms of the global morphology (e.g., twisted filament, helical ribbon, and nanotube) but also with respect to the number of protofilaments within a given peptide assembly. These results suggest that the folding landscape of PSM derivatives may be more complex than originally anticipated and that the assemblies are able to sample a wide range of supramolecular structural space.
MeSH term(s)	Amyloid/chemistry ; Bacterial Toxins ; Cryoelectron Microscopy ; Humans ; Nanotubes ; Peptides/chemistry ; Staphylococcus aureus/metabolism
Chemical Substances	Amyloid ; Bacterial Toxins ; Peptides ; staphylococcal delta toxin
Language	English
Publishing date	2022-05-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2121586119
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Article ; Online: Archaeal DNA-import apparatus is homologous to bacterial conjugation machinery.

Beltran, Leticia C / Cvirkaite-Krupovic, Virginija / Miller, Jessalyn / Wang, Fengbin / Kreutzberger, Mark A B / Patkowski, Jonasz B / Costa, Tiago R D / Schouten, Stefan / Levental, Ilya / Conticello, Vincent P / Egelman, Edward H / Krupovic, Mart

Nature communications

2023 Volume 14, Issue 1, Page(s) 666

Abstract: Conjugation is a major mechanism of horizontal gene transfer promoting the spread of antibiotic resistance among human pathogens. It involves establishing a junction between a donor and a recipient cell via an extracellular appendage known as the mating ... ...

Abstract	Conjugation is a major mechanism of horizontal gene transfer promoting the spread of antibiotic resistance among human pathogens. It involves establishing a junction between a donor and a recipient cell via an extracellular appendage known as the mating pilus. In bacteria, the conjugation machinery is encoded by plasmids or transposons and typically mediates the transfer of cognate mobile genetic elements. Much less is known about conjugation in archaea. Here, we determine atomic structures by cryo-electron microscopy of three conjugative pili, two from hyperthermophilic archaea (Aeropyrum pernix and Pyrobaculum calidifontis) and one encoded by the Ti plasmid of the bacterium Agrobacterium tumefaciens, and show that the archaeal pili are homologous to bacterial mating pili. However, the archaeal conjugation machinery, known as Ced, has been 'domesticated', that is, the genes for the conjugation machinery are encoded on the chromosome rather than on mobile genetic elements, and mediates the transfer of cellular DNA.
MeSH term(s)	Agrobacterium tumefaciens/genetics ; Bacterial Proteins/genetics ; Conjugation, Genetic ; Cryoelectron Microscopy ; DNA, Archaeal/genetics ; DNA, Bacterial/genetics ; Gene Transfer, Horizontal ; Plasmids ; Aeropyrum/genetics ; Pyrobaculum/genetics
Chemical Substances	Bacterial Proteins ; DNA, Archaeal ; DNA, Bacterial
Language	English
Publishing date	2023-02-07
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-36349-8
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Geometrical frustration as a potential design principle for peptide-based assemblies.

Jiang, Tao / Magnotti, Elizabeth L / Conticello, Vincent P

Interface focus

2017 Volume 7, Issue 6, Page(s) 20160141

Abstract: Two-dimensional peptide and protein assemblies have been the focus of increased scientific research as they display significant potential for the creation of functional nanomaterials. Soluble subunits derived from a variety of protein motifs have been ... ...

Abstract	Two-dimensional peptide and protein assemblies have been the focus of increased scientific research as they display significant potential for the creation of functional nanomaterials. Soluble subunits derived from a variety of protein motifs have been demonstrated to self-assemble into structurally defined nanosheets under environmentally benign conditions in which the components often retain their native structure and function. These types of two-dimensional assemblies may have an advantage for nanofabrication in that their extended planar shapes can be more straightforwardly incorporated into the current formats of nanoscale devices. However, significant challenges remain in the fabrication of these materials, particularly in devising methods to control the size, shape and internal structure of the resultant materials. Geometrical frustration may be envisioned as a possible mechanism to exert control over these structural parameters through rational design. While this objective has yet to be realized in practice, we discuss in this article the potential role of geometrical frustration as a principle to rationalize unusual self-assembly behaviour in several examples of two-dimensional peptide assemblies.
Language	English
Publishing date	2017-10-20
Publishing country	England
Document type	Journal Article ; Review
ISSN	2042-8898
ISSN	2042-8898
DOI	10.1098/rsfs.2016.0141
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Article ; Online: Deterministic chaos in the self-assembly of β sheet nanotubes from an amphipathic oligopeptide.

Wang, Fengbin / Gnewou, Ordy / Wang, Shengyuan / Osinski, Tomasz / Zuo, Xiaobing / Egelman, Edward H / Conticello, Vincent P

Matter

2021 Volume 4, Issue 10, Page(s) 3217–3231

Abstract: The self-assembly of designed peptides into filaments and other higher-order structures has been the focus of intense interest because of the potential for creating new biomaterials and biomedical devices. These peptide assemblies have also been used as ... ...

Abstract	The self-assembly of designed peptides into filaments and other higher-order structures has been the focus of intense interest because of the potential for creating new biomaterials and biomedical devices. These peptide assemblies have also been used as models for understanding biological processes, such as the pathological formation of amyloid. We investigate the assembly of an octapeptide sequence, Ac-FKFEFKFE-NH
Language	English
Publishing date	2021-07-27
Publishing country	United States
Document type	Journal Article
ISSN	2590-2385
ISSN (online)	2590-2385
DOI	10.1016/j.matt.2021.06.037
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Article ; Online: Design of Multicomponent Peptide Fibrils with Ordered and Programmable Compositional Patterns.

Cheng, Dan / Chen, Xin / Zhang, Weijia / Guo, Pan / Xue, Wenhui / Xia, Junfan / Wu, Siyu / Shi, Junhui / Ma, Dan / Zuo, Xiaobing / Jiang, Bin / Li, Shaowei / Xia, Ningshao / Jiang, Yunbao / Conticello, Vincent P / Jiang, Tao

Angewandte Chemie (International ed. in English)

2023 Volume 62, Issue 22, Page(s) e202303684

Abstract: Advanced applications of biomacromolecular assemblies require a stringent degree of control over molecular arrangement, which is a challenge to current synthetic methods. Here we used a neighbor-controlled patterning strategy to build multicomponent ... ...

Abstract	Advanced applications of biomacromolecular assemblies require a stringent degree of control over molecular arrangement, which is a challenge to current synthetic methods. Here we used a neighbor-controlled patterning strategy to build multicomponent peptide fibrils with an unprecedented capacity to manipulate local composition and peptide positions. Eight peptides were designed to have regulable nearest neighbors upon co-assembly, which, by simulation, afforded 412 different patterns within fibrils, with varied compositions and/or peptide positions. The fibrils with six prescribed patterns were experimentally constructed with high accuracy. The controlled patterning also applies to functionalities appended to the peptides, as exemplified by arranging carbohydrate ligands at nanoscale precision for protein recognition. This study offers a route to molecular editing of inner structures of peptide assemblies, prefiguring the uniqueness and richness of patterning-based material design.
MeSH term(s)	Peptides/chemistry ; Proteins ; Molecular Conformation
Chemical Substances	Peptides ; Proteins
Language	English
Publishing date	2023-04-25
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2011836-3
ISSN	1521-3773 ; 1433-7851
ISSN (online)	1521-3773
ISSN	1433-7851
DOI	10.1002/anie.202303684
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Article: Structurally Ordered Nanowire Formation from Co-Assembly of DNA Origami and Collagen-Mimetic Peptides

Jiang, Tao / Conticello Vincent P / Ke Yonggang / Meyer Travis A / Modlin Charles / Zuo Xiaobing

Journal of the American Chemical Society. 2017 Oct. 11, v. 139, no. 40

2017

Abstract: We describe the co-assembly of two different building units: collagen-mimetic peptides and DNA origami. Two peptides CP++ and sCP++ are designed with a sequence comprising a central block (Pro-Hyp-Gly) and two positively charged domains (Pro-Arg-Gly) at ... ...

Abstract	We describe the co-assembly of two different building units: collagen-mimetic peptides and DNA origami. Two peptides CP++ and sCP++ are designed with a sequence comprising a central block (Pro-Hyp-Gly) and two positively charged domains (Pro-Arg-Gly) at both N- and C-termini. Co-assembly of peptides and DNA origami two-layer (TL) nanosheets affords the formation of one-dimensional nanowires with repeating periodicity of ∼10 nm. Structural analyses suggest a face-to-face stacking of DNA nanosheets with peptides aligned perpendicularly to the sheet surfaces. We demonstrate the potential of selective peptide-DNA association between face-to-face and edge-to-edge packing by tailoring the size of DNA nanostructures. This study presents an attractive strategy to create hybrid biomolecular assemblies from peptide- and DNA-based building blocks that takes advantage of the intrinsic chemical and physical properties of the respective components to encode structural and, potentially, functional complexity within readily accessible biomimetic materials.
Keywords	biomimetic materials ; DNA ; nanosheets ; nanowires ; peptides ; periodicity ; physical properties
Language	English
Dates of publication	2017-1011
Size	p. 14025-14028.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021%2Fjacs.7b08087
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