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Full Record Details
Persistent URL
http://purl.org/net/epubs/work/53451257
Record Status
Checked
Record Id
53451257
Title
Peptide Self-Assemblies from Unusual α-Sheet Conformations Based on Alternation of D/L Amino Acids
Contributors
P Zhou (State Key Laboratory of Heavy Oil Processing and Department of Biological and Energy Chemical Engineering)
,
X Hu (Biological Physics Group)
,
J Li (State Key Laboratory of Heavy Oil Processing and Department of Biological and Energy Chemical Engineering)
,
Y Wang (State Key Laboratory of Heavy Oil Processing and Department of Biological and Energy Chemical Engineering)
,
H Yu (State Key Laboratory of Heavy Oil Processing and Department of Biological and Energy Chemical Engineering)
,
Z Chen (State Key Laboratory of Heavy Oil Processing and Department of Biological and Energy Chemical Engineering)
,
D Wang (State Key Laboratory of Heavy Oil Processing and Department of Biological and Energy Chemical Engineering)
,
Y Zhao (State Key Laboratory of Heavy Oil Processing and Department of Biological and Energy Chemical Engineering)
,
SM King (STFC Rutherford Appleton Lab.)
,
SE Rogers (STFC Rutherford Appleton Lab.)
,
J Wang (State Key Laboratory of Heavy Oil Processing and Department of Biological and Energy Chemical Engineering)
,
JR Lu (Biological Physics Group)
,
H Xu (State Key Laboratory of Heavy Oil Processing and Department of Biological and Energy Chemical Engineering)
Abstract
Peptide self-assembly is a hierarchical process during which secondary structures formed in the initial stages play a critical role in determining the subsequent assembling processes and final structural ordering. Unusual secondary structures hold promise as a source to develop novel supramolecular architectures with unique properties. In this work, we report the design of a new peptide self-assembly strategy based on unusual α-sheet secondary structures. In light of the strong propensity of leucine toward forming helical conformations and its high hydrophobicity, we design two short amphiphilic peptides Ac-LDLLDLK-NH2 and Ac-DLLDLLDK-NH2 with alternating l- and d-form amino acids. Microscopic imaging, neutron scattering, and spectroscopic measurements indicate that the two heterochiral peptides form highly ordered wide nanotubes and helical ribbons with monolayer thickness, in sharp contrast to twisted nanofibrils formed by the homochiral peptide Ac-LLLLK-NH2. Molecular dynamics simulations from monomers to trimers reveal that the two heteropeptides fold into α-sheets instead of β-sheets, which readily pack into tubular architectures in oligomer simulations. Simulated circular dichroism spectra based on α-sheet oligomers validate the proposed α-sheet secondary structures. These results form an important basis for the rational design of higher-order peptide assemblies with novel properties based on unusual α-sheet secondary structures.
Organisation
ISIS
,
ISIS-LOQ
,
STFC
Keywords
Funding Information
China Postdoctoral Science Foundation
(2021M693205);
Innovate UK
(KTP12697);
NNSFC
(22072181);
NNSFC
(22172193);
NNSFC
(U1832108);
Syngenta
(KTP12697)
Related Research Object(s):
Licence Information:
Language
English (EN)
Type
Details
URI(s)
Local file(s)
Year
Journal Article
J Am Chem Soc
144, no. 47 (2022): 21544-21554.
doi:10.1021/jacs.2c08425
2022
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