Interplay between Intrinsic Conformational Propensities and Intermolecular Interactions in the Self-Assembly of Short Surfactant-like Peptides Composed of Leucine/Isoleucine
文献类型：期刊论文
| 作者 | 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.; 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.
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| 刊名 | LANGMUIR
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| 出版日期 | 2016 |
| 卷号 | 32期号:18页码:4662-4672 |
| DOI | http://dx.doi.org/10.1021/acs.langmuir.6b00287 |
| 英文摘要 | 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. |
| 学科主题 | Chemistry ; Materials Science |
| 语种 | 英语 |
| 源URL | [http://ir.itp.ac.cn/handle/311006/21656]  |
| 专题 | 理论物理研究所_理论物理所1978-2010年知识产出 计算平台成果 |
| 通讯作者 | 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.; 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. |
| 推荐引用方式 GB/T 7714 | Wang, YT ,Lu, JR ,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[J]. LANGMUIR,2016,32(18):4662-4672. |
| APA | Wang, YT .,Lu, JR .,Zhou, P.,Deng, L.,Wang, YT.,...&Xu, H .(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 | 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".LANGMUIR 32.18(2016):4662-4672. |
入库方式： OAI收割
来源：理论物理研究所
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