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Interplay between Intrinsic Conformational Propensities and Intermolecular Interactions in the Self-Assembly of Short Surfactant-like Peptides Composed of Leucine/Isoleucine
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.
2016
发表期刊LANGMUIR
卷号32期号:18页码:4662-4672
文章类型Article
摘要To 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.
合作性质国际
学科领域Chemistry ; Materials Science
资助者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] ; National Natural Science Foundation of China [21373270, 11504431, 11421063] ; China Scholarship Council ; China Scholarship Council ; China Scholarship Council ; China Scholarship Council ; 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] ; National Natural Science Foundation of China [21373270, 11504431, 11421063] ; China Scholarship Council ; China Scholarship Council ; China Scholarship Council ; China Scholarship Council
DOIhttp://dx.doi.org/10.1021/acs.langmuir.6b00287
关键词[WOS]SECONDARY STRUCTURE ; BLOCKED DIPEPTIDES ; POLYPROLINE-II ; PROTEINS ; WATER ; NANOSTRUCTURES ; TRANSITIONS ; FABRICATION ; NANOTUBES ; MOLECULES
收录类别SCI
语种英语
资助者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] ; National Natural Science Foundation of China [21373270, 11504431, 11421063] ; China Scholarship Council ; China Scholarship Council ; China Scholarship Council ; China Scholarship Council ; 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] ; National Natural Science Foundation of China [21373270, 11504431, 11421063] ; China Scholarship Council ; China Scholarship Council ; China Scholarship Council ; China Scholarship Council
WOS类目Chemistry, Multidisciplinary ; Chemistry, Physical ; Materials Science, Multidisciplinary
引用统计
文献类型期刊论文
条目标识符http://ir.itp.ac.cn/handle/311006/21237
专题计算平台成果
通讯作者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.
推荐引用方式
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.
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