skip to main content
DOE PAGES title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Self-Assembly of an α-Helical Peptide into a Crystalline Two-Dimensional Nanoporous Framework

Abstract

Sequence-specific peptides have been demonstrated to self-assemble into structurally defined nano-scale ob-jects including nanofibers, nanotubes, and nanosheets. The latter structures display significant promise for the construction of hybrid materials for functional devices due to their extended planar geometry. Realization of this objective necessitates the ability to control the structural features of the resultant assemblies through the peptide sequence. The design of a amphiphilic peptide, 3FD-IL, is described that comprises two repeats of a canonical 18 amino acid sequence associated with straight xhelical structures. Peptide 3FD-IL displays three-fold screw symmetry in a helical conformation and self-assem-bles into nanosheets based on hexagonal packing of helices. Biophysical evidence from TEM, cryo-TEM, SAXS, AFM, and STEM measurements on the 3FD-IL nanosheets support a structural model based on a honeycomb lattice, in which the length of the peptide determines the thickness of the nanosheet and the packing of helices defines the presence of nanoscale channels that permeate the sheet. The honeycomb structure can be rationalized on the basis of geometrical packing frus-tration in which the channels occupy defect sites that define a periodic super-lattice. The resultant 2D materials may have potential as materials for nanoscale transport and controlled release applications.

Authors:
 [1];  [1];  [2];  [1];  [1];  [1]; ORCiD logo [1];  [3];  [4];  [2];  [1]
  1. Emory Univ., Atlanta, GA (United States). Dept. of Chemistry
  2. Emory Univ., Atlanta, GA (United States). School of Medicine, Dept. of Pediatrics
  3. Brookhaven National Lab. (BNL), Upton, NY (United States)
  4. Argonne National Lab. (ANL), Argonne, IL (United States). X-ray Science Division
Publication Date:
Research Org.:
Brookhaven National Lab. (BNL), Upton, NY (United States); Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Biological and Environmental Research (BER); National Institutes of Health (NIH); USDOE Office of Science (SC), Basic Energy Sciences (BES)
OSTI Identifier:
1351722
Alternate Identifier(s):
OSTI ID: 1373400
Report Number(s):
BNL-113693-2017-JA
Journal ID: ISSN 0002-7863
Grant/Contract Number:  
SC0012704; W-31-109-Eng-38; S10RR025679; R01GM104540; UL1TR000454; CHE-1309817; CHE-1012620; CHE-1412580; AC02-06CH11357
Resource Type:
Accepted Manuscript
Journal Name:
Journal of the American Chemical Society
Additional Journal Information:
Journal Volume: 138; Journal Issue: 50; Journal ID: ISSN 0002-7863
Publisher:
American Chemical Society (ACS)
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; 59 BASIC BIOLOGICAL SCIENCES; Peptide design; self-assembly; nanosheet; porus material; honeycomb structure; porous material

Citation Formats

Magnotti, Elizabeth L., Hughes, Spencer A., Dillard, Rebecca S., Wang, Shengyuan, Hough, Lillian, Karumbamkandathil, Arshad, Lian, Tianquan, Wall, Joseph S., Zuo, Xiaobing, Wright, Elizabeth R., and Conticello, Vincent P. Self-Assembly of an α-Helical Peptide into a Crystalline Two-Dimensional Nanoporous Framework. United States: N. p., 2016. Web. doi:10.1021/jacs.6b06592.
Magnotti, Elizabeth L., Hughes, Spencer A., Dillard, Rebecca S., Wang, Shengyuan, Hough, Lillian, Karumbamkandathil, Arshad, Lian, Tianquan, Wall, Joseph S., Zuo, Xiaobing, Wright, Elizabeth R., & Conticello, Vincent P. Self-Assembly of an α-Helical Peptide into a Crystalline Two-Dimensional Nanoporous Framework. United States. doi:10.1021/jacs.6b06592.
Magnotti, Elizabeth L., Hughes, Spencer A., Dillard, Rebecca S., Wang, Shengyuan, Hough, Lillian, Karumbamkandathil, Arshad, Lian, Tianquan, Wall, Joseph S., Zuo, Xiaobing, Wright, Elizabeth R., and Conticello, Vincent P. Tue . "Self-Assembly of an α-Helical Peptide into a Crystalline Two-Dimensional Nanoporous Framework". United States. doi:10.1021/jacs.6b06592. https://www.osti.gov/servlets/purl/1351722.
@article{osti_1351722,
title = {Self-Assembly of an α-Helical Peptide into a Crystalline Two-Dimensional Nanoporous Framework},
author = {Magnotti, Elizabeth L. and Hughes, Spencer A. and Dillard, Rebecca S. and Wang, Shengyuan and Hough, Lillian and Karumbamkandathil, Arshad and Lian, Tianquan and Wall, Joseph S. and Zuo, Xiaobing and Wright, Elizabeth R. and Conticello, Vincent P.},
abstractNote = {Sequence-specific peptides have been demonstrated to self-assemble into structurally defined nano-scale ob-jects including nanofibers, nanotubes, and nanosheets. The latter structures display significant promise for the construction of hybrid materials for functional devices due to their extended planar geometry. Realization of this objective necessitates the ability to control the structural features of the resultant assemblies through the peptide sequence. The design of a amphiphilic peptide, 3FD-IL, is described that comprises two repeats of a canonical 18 amino acid sequence associated with straight xhelical structures. Peptide 3FD-IL displays three-fold screw symmetry in a helical conformation and self-assem-bles into nanosheets based on hexagonal packing of helices. Biophysical evidence from TEM, cryo-TEM, SAXS, AFM, and STEM measurements on the 3FD-IL nanosheets support a structural model based on a honeycomb lattice, in which the length of the peptide determines the thickness of the nanosheet and the packing of helices defines the presence of nanoscale channels that permeate the sheet. The honeycomb structure can be rationalized on the basis of geometrical packing frus-tration in which the channels occupy defect sites that define a periodic super-lattice. The resultant 2D materials may have potential as materials for nanoscale transport and controlled release applications.},
doi = {10.1021/jacs.6b06592},
journal = {Journal of the American Chemical Society},
number = 50,
volume = 138,
place = {United States},
year = {2016},
month = {11}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record

Citation Metrics:
Cited by: 6 works
Citation information provided by
Web of Science

Save / Share:

Works referencing / citing this record:

Comparing proteins and nucleic acids for next-generation biomolecular engineering
journal, July 2018

  • Pugh, Genevieve C.; Burns, Jonathan R.; Howorka, Stefan
  • Nature Reviews Chemistry, Vol. 2, Issue 7
  • DOI: 10.1038/s41570-018-0015-9

Comparing proteins and nucleic acids for next-generation biomolecular engineering
journal, July 2018

  • Pugh, Genevieve C.; Burns, Jonathan R.; Howorka, Stefan
  • Nature Reviews Chemistry, Vol. 2, Issue 7
  • DOI: 10.1038/s41570-018-0015-9

Precise Self‐Assembly of Nanoparticles into Ordered Nanoarchitectures Directed by Tobacco Mosaic Virus Coat Protein
journal, March 2019


2D Crystal Engineering of Nanosheets Assembled from Helical Peptide Building Blocks
journal, August 2019

  • Merg, Andrea D.; Touponse, Gavin; van Genderen, Eric
  • Angewandte Chemie, Vol. 131, Issue 38
  • DOI: 10.1002/ange.201906214

Pillar[5]arene-Based Supramolecular Organic Framework with Multi-Guest Detection and Recyclable Separation Properties
journal, December 2017

  • Lin, Qi; Fan, Yan-Qing; Mao, Peng-Peng
  • Chemistry - A European Journal, Vol. 24, Issue 4
  • DOI: 10.1002/chem.201705107

The art of two-dimensional soft nanomaterials
journal, June 2019


The design and biomedical applications of self-assembled two-dimensional organic biomaterials
journal, January 2019

  • Zhang, Xiaoyuan; Gong, Coucong; Akakuru, Ozioma Udochukwu
  • Chemical Society Reviews, Vol. 48, Issue 23
  • DOI: 10.1039/c8cs01003j

Designing phenylalanine-based hybrid biological materials: controlling morphology via molecular composition
journal, January 2018

  • Mushnoori, Srinivas; Schmidt, Kassandra; Nanda, Vikas
  • Organic & Biomolecular Chemistry, Vol. 16, Issue 14
  • DOI: 10.1039/c8ob00130h

Degradation of phthalic acid esters (PAEs) by an enzyme mimic and its application in the degradation of intracellular DEHP
journal, January 2019

  • Li, Xia; Li, Jianpeng; Zhu, Junxiang
  • Chemical Communications, Vol. 55, Issue 89
  • DOI: 10.1039/c9cc06794a