Interplay between Intrinsic Conformational Propensities and Intermolecular Interactions in the Self-Assembly of Short Surfactant-like Peptides Composed of Leucine/Isoleucine

doi:http://dx.doi.org/10.1021/acs.langmuir.6b00287

CORC > 理论物理研究所 > 中国科学院理论物理研究所 > 理论物理所科研产出 > 理论物理所1978-2010年知识产出

	Interplay between Intrinsic Conformational Propensities and Intermolecular Interactions in the Self-Assembly of Short Surfactant-like Peptides Composed of Leucine/Isoleucine
	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.
刊名	LANGMUIR
	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
内容类型	期刊论文
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
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.