ITP OpenIR  > 理论物理所科研产出  > SCI论文
Zhou, P; Deng, L; Wang, YT; Lu, JR; Xu, H; Xu, H (reprint author), China Univ Petr East China, State Key Lab Heavy Oil Proc, 66 Changjiang West Rd, Qingdao, Peoples R China.; Xu, H (reprint author), China Univ Petr East China, Ctr Bioengn & Biotechnol, 66 Changjiang West Rd, Qingdao, Peoples R China.; Wang, YT (reprint author), Chinese Acad Sci, Inst Theoret Phys, 55 East Zhongguancun Rd, Beijing, Peoples R China.; Lu, JR (reprint author), Univ Manchester Inst, Sch Phys & Astron, Phys Biol Lab, Manchester M13 9PL, Lancs, England.
Interplay between Intrinsic Conformational Propensities and Intermolecular Interactions in the Self-Assembly of Short Surfactant-like Peptides Composed of Leucine/Isoleucine
Source PublicationLANGMUIR
Language英语
AbstractTo study how the conformational propensities of individual amino acid residues, primary structures (i.e., adjacent residues and molecular lengths), and intermolecular interactions of peptides affect their self-assembly properties, we report the use of replica exchange molecular dynamics (REMD) to investigate the monomers, dialers, and trimers of a series of short surfactant-like peptides (I3K, L3K, L4K, and L5K). For four-residue peptides X3K (I3K and L3K), the results show that their different aggregation behaviors arise from the different intrinsic conformational propensities of isoleucine and leucine. For LmK peptides (L3K, L4K, and L5K), the molecular length is found to dictate their aggregation via primarily modulating intermolecular interactions. Increasing the number of hydrophobic amino acid residues of LmK peptides enhances their intermolecular H-bonding and promotes the formation of beta-strands in dimer and trimer aggregates, overwhelming the intrinsic preference of Leu for helical structures. Thus, the interplay between the conformational propensities of individual amino acid residues for secondary structures and molecular interactions determines the self-assembly properties of the peptides, and the competition between intramolecular and intermolecular H-bonding interactions determines the probability of beta-sheet alignment of peptide molecules. These results are validated by comparing simulated and experimental CD spectra of the peptides. This study will aid the design of short peptide amphiphiles and improve the mechanistic understanding of their self-assembly behavior.
2016
Volume32Issue:18Pages:4662-4672
Subject AreaChemistry ; Materials Science
DOIhttp://dx.doi.org/10.1021/acs.langmuir.6b00287
Indexed BySCI
Funding OrganizationNational Natural Science Foundation of China [21373270, 11504431, 11421063] ; National Natural Science Foundation of China [21373270, 11504431, 11421063] ; National Natural Science Foundation of China [21373270, 11504431, 11421063] ; National Natural Science Foundation of China [21373270, 11504431, 11421063] ; China Scholarship Council ; China Scholarship Council ; China Scholarship Council ; China Scholarship Council
Citation statistics
Document Type期刊论文
Identifierhttp://ir.itp.ac.cn/handle/311006/21656
Collection理论物理所科研产出_SCI论文
Corresponding AuthorXu, H (reprint author), China Univ Petr East China, State Key Lab Heavy Oil Proc, 66 Changjiang West Rd, Qingdao, Peoples R China.; Xu, H (reprint author), China Univ Petr East China, Ctr Bioengn & Biotechnol, 66 Changjiang West Rd, Qingdao, Peoples R China.; Wang, YT (reprint author), Chinese Acad Sci, Inst Theoret Phys, 55 East Zhongguancun Rd, Beijing, Peoples R China.; Lu, JR (reprint author), Univ Manchester Inst, Sch Phys & Astron, Phys Biol Lab, Manchester M13 9PL, Lancs, England.
Recommended Citation
GB/T 7714
Zhou, P,Deng, L,Wang, YT,et al. Interplay between Intrinsic Conformational Propensities and Intermolecular Interactions in the Self-Assembly of Short Surfactant-like Peptides Composed of Leucine/Isoleucine[J]. LANGMUIR,2016,32(18):4662-4672.
APA Zhou, P.,Deng, L.,Wang, YT.,Lu, JR.,Xu, H.,...&Lu, JR .(2016).Interplay between Intrinsic Conformational Propensities and Intermolecular Interactions in the Self-Assembly of Short Surfactant-like Peptides Composed of Leucine/Isoleucine.LANGMUIR,32(18),4662-4672.
MLA Zhou, P,et al."Interplay between Intrinsic Conformational Propensities and Intermolecular Interactions in the Self-Assembly of Short Surfactant-like Peptides Composed of Leucine/Isoleucine".LANGMUIR 32.18(2016):4662-4672.
Files in This Item:
File Name/Size DocType Version Access License
Interplay between in(2263KB) 开放获取--Application Full Text
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Google Scholar
Similar articles in Google Scholar
[Zhou, P]'s Articles
[Deng, L]'s Articles
[Wang, YT]'s Articles
Baidu academic
Similar articles in Baidu academic
[Zhou, P]'s Articles
[Deng, L]'s Articles
[Wang, YT]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Zhou, P]'s Articles
[Deng, L]'s Articles
[Wang, YT]'s Articles
Terms of Use
No data!
Social Bookmark/Share
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.