State Key Laboratory of Heavy Oil Processing and Centre for Bioengineering and Biotechnology, China University of Petroleum (East China), 66 Changjiang West Road, Qingdao, China; School of Petroleum Engineering and Key Laboratory of Unconventional Oil & Gas Development of Education Ministry, China University of Petroleum (East China), 66 Changjiang West Road, Qingdao, China.
State Key Laboratory of Heavy Oil Processing and Centre for Bioengineering and Biotechnology, China University of Petroleum (East China), 66 Changjiang West Road, Qingdao, China.
J Colloid Interface Sci. 2019 Jul 15;548:244-254. doi: 10.1016/j.jcis.2019.04.019. Epub 2019 Apr 6.
A variety of nanostructures with different chiral features can be self-assembled from short peptides with highly similar sequences. We hypothesize that these supramolecular nanostructures are ruled by the constituent amino acid residues which adopt their conformations under the influence of intra-/inter-molecular interactions during peptide self-assembly.
Through reviewing recent advances in the self-assembly of short peptides and focusing on the relationship between amino acid conformations, peptide secondary structures and intra-/inter-molecular interactions within the supramolecular architectures, we aim to rationalize the complex interactive processes involved in the self-assembly of short, designed peptides.
Given the highly complexing interactive processes, the adoption of amino acid conformations and their control over peptide self-assembly consist of 4 main steps: (1) Each amino acid residue adopts its unique conformation in a specific sequence; (2) The sequence exhibits its own main chain geometry and determines the propensity of the intermolecular alignment within the building block; (3) The structural propensity of the building block and the packing mode between them determine the self-assembled structural features such as twisting, growth and chirality; (4) In addition to intra-/inter-molecular interactions, inter-sheet and inter-building block interactions could also affect the residue conformations and nanostructures, causing structural readjustment.
具有不同手性特征的各种纳米结构可以由高度相似序列的短肽自组装而成。我们假设这些超分子纳米结构由组成氨基酸残基决定，这些氨基酸残基在肽自组装过程中受到分子内/分子间相互作用的影响，从而采用其构象。
通过回顾短肽自组装的最新进展，并重点关注氨基酸构象、肽二级结构和超分子结构内的分子内/分子间相互作用之间的关系，我们旨在合理化涉及短肽的复杂相互作用过程设计。
鉴于高度复杂的相互作用过程，氨基酸构象的采用及其对肽自组装的控制由 4 个主要步骤组成：（1）每个氨基酸残基在特定序列中采用其独特的构象；（2）该序列表现出其自身的主链几何形状，并确定构建块内分子间排列的倾向；（3）构建块的结构倾向和它们之间的堆积模式决定了自组装结构特征，如扭曲、生长和手性；（4）除了分子内/分子间相互作用外，层间和构建块间相互作用也可能影响残基构象和纳米结构，导致结构调整。
