Univ. Lyon, ENS de Lyon, CNRS UMR 5182, Université Claude Bernard Lyon 1, Laboratoire de Chimie, F69342, Lyon, France.
Université de Paris, Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques, UMR CNRS 8601, Paris, France.
Phys Chem Chem Phys. 2021 May 19;23(19):11224-11232. doi: 10.1039/d0cp06570f.
In the realm of biomolecules, peptides can present a large diversity of structures. Our study sheds new light on the structural interplay between a tris-dipicolinate lanthanide probe and a decapeptide SASYKTLPRG. Although a rather trivial, electrostatically driven interaction was expected, the combination of paramagnetic NMR and molecular dynamics simulations reveals a highly dynamic association process and allows for providing extensive insights into the interaction sites and their occupancy. This study highlights the importance of a large conformational sampling to reconcile characteristic time in NMR with molecular dynamics simulations, where sampling in the microsecond range is needed. This study opens the door for a detailed mechanistic elucidation of the early steps of lanthanide complex-peptide or lanthanide complex-protein interaction or self-assembly processes.
在生物分子领域，多肽可以呈现出多种多样的结构。我们的研究揭示了三齿二吡啶酸镧系探针与十肽 SASYKTLPRG 之间结构相互作用的新情况。尽管预期这是一种相当简单的、静电驱动的相互作用，但顺磁 NMR 和分子动力学模拟的结合揭示了一个高度动态的结合过程，并允许对相互作用位点及其占据情况进行广泛的了解。这项研究强调了进行大构象采样以协调 NMR 中的特征时间与分子动力学模拟的重要性，其中需要在微秒范围内进行采样。这项研究为详细阐明镧系配合物-肽或镧系配合物-蛋白质相互作用或自组装过程的早期步骤开辟了道路。
