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Tytuł:
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Exploiting terminal charged residue shift for wide bilayer nanotube assembly.
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Autorzy:
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Zhao Y; State Key Laboratory of Heavy Oil Processing and Department of Biological and Energy Engineering, China University of Petroleum (East China), 66 Changjiang West Road, Qingdao 266580, China. Electronic address: .
Qi H; State Key Laboratory of Heavy Oil Processing and Department of Biological and Energy Engineering, China University of Petroleum (East China), 66 Changjiang West Road, Qingdao 266580, China.
Zhang L; State Key Laboratory of Heavy Oil Processing and Department of Biological and Energy Engineering, China University of Petroleum (East China), 66 Changjiang West Road, Qingdao 266580, China.
He C; Spallation Neutron Source Science Center, Dalang, Dongguan 523803, China; Institute of High Energy Physics, Chinese Academy of Sciences (CAS), Beijing 100049, China.
Wei F; State Key Laboratory of Heavy Oil Processing and Department of Biological and Energy Engineering, China University of Petroleum (East China), 66 Changjiang West Road, Qingdao 266580, China.
Wang D; State Key Laboratory of Heavy Oil Processing and Department of Biological and Energy Engineering, China University of Petroleum (East China), 66 Changjiang West Road, Qingdao 266580, China.
Li J; College of Life Science, Nankai University, Tianjin 300071, China.
Qi K; State Key Laboratory of Heavy Oil Processing and Department of Biological and Energy Engineering, China University of Petroleum (East China), 66 Changjiang West Road, Qingdao 266580, China.
Hu X; Biological Physics Group, Department of Physics and Astronomy, The University of Manchester, Manchester M13 9PL, United Kingdom.
Wang J; State Key Laboratory of Heavy Oil Processing and Department of Biological and Energy Engineering, China University of Petroleum (East China), 66 Changjiang West Road, Qingdao 266580, China.
Ke Y; Spallation Neutron Source Science Center, Dalang, Dongguan 523803, China; Institute of High Energy Physics, Chinese Academy of Sciences (CAS), Beijing 100049, China.
Zhang C; College of Life Science, Nankai University, Tianjin 300071, China.
Lu JR; Biological Physics Group, Department of Physics and Astronomy, The University of Manchester, Manchester M13 9PL, United Kingdom.
Xu H; State Key Laboratory of Heavy Oil Processing and Department of Biological and Energy Engineering, China University of Petroleum (East China), 66 Changjiang West Road, Qingdao 266580, China. Electronic address: .
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Źródło:
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Journal of colloid and interface science [J Colloid Interface Sci] 2023 Jan; Vol. 629 (Pt A), pp. 1-10. Date of Electronic Publication: 2022 Aug 17.
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Typ publikacji:
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Journal Article
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Język:
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English
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Imprint Name(s):
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Publication: Orlando, FL : Academic Press
Original Publication: New York.
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MeSH Terms:
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Nanotubes, Peptide*
Nanotubes*/chemistry
Protein Structure, Secondary ; Lysine ; Peptides/chemistry
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Contributed Indexing:
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Keywords: Dimerization; Self-assembly; Short amphiphilic peptide; Terminal residue shift; Thin nanofibril; Wide nanotube
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Substance Nomenclature:
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0 (Nanotubes, Peptide)
K3Z4F929H6 (Lysine)
0 (Peptides)
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Entry Date(s):
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Date Created: 20220901 Date Completed: 20221027 Latest Revision: 20221027
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Update Code:
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20240105
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DOI:
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10.1016/j.jcis.2022.08.104
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PMID:
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36049324
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Hypothesis: Self-assembly of peptides is influenced by both molecular structure and external conditions, which dictate the delicate balance of different non-covalent interactions that driving the self-assembling process. The shifting of terminal charge residue is expected to influence the non-covalent interactions and their interplay, thereby affecting the morphologies of self-assemblies. Therefore, the morphology transition can be realized by shifting the position of the terminal charge residue.
Experiments: The structure transition from thin nanofibers to giant nanotubes is realized by simply shifting the C-terminal lysine of ultrashort Ac-I 3 K-NH 2 to its N-terminus. The morphologies and detailed structure information of the self-assemblies formed by these two peptides are investigated systemically by a combination of different experimental techniques. The effect of terminal residue on the morphologies of the self-assemblies is well presented and the underlying mechanism is revealed.
Findings: Giant nanotubes with a bilayer shell structure can be self-assembled by the ultrashort peptide Ac-KI 3 -NH 2 with the lysine residue close to the N-terminal. The Ac-KI 3 -NH 2 dimerization through intermolecular C-terminal H-bonding promotes the formation of a bola-form geometry, which is responsible for the wide nanotube assembly formation. The evolution process of Ac-KI 3 -NH 2 nanotubes follows the "growing width" model. Such a morphological transformation with the terminal lysine shift is applicable to other analogues and thus provides a facile approach for the self-assembly of wide peptide nanotubes, which can expand the library of good template structures for the prediction of peptide nanostructures.
Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2022 Elsevier Inc. All rights reserved.)
