Fang Ya-Yin, Morris Vernon R, Lingani Guy M, Long Eric C, Southerland William M
Department of Biochemistry & Molecular Biology, Howard University College of Medicine, Washington, DC 20059, USA.
Open Conf Proc J. 2010;1:157-163. doi: 10.2174/22102892010010100157.
Knowledge of the sequence of the human genome has provided significant opportunities to exploit DNA as a target in the rational design of therapeutic agents. Among agents that target DNA, netropsin exhibits a strong preference for binding A/T rich regions. In order to investigate the key factors responsible for DNA recognition and binding by netropsin, molecular dynamics simulations were carried out on a DNA-netropsin complex in which two netropsin molecules are bound to each AATT site of the 16-mer d(CTTAATTCGAATTAAG)(2). In this complex, the two netropsins are bound to the DNA minor groove in a head-to-head orientation with the guanidinium-termini of both netropsins pointed toward the center of the DNA. Despite their identical environments, molecular dynamics simulations showed that the two netropsins exhibited differences in their respective RMS behaviors, binding energies, minor groove width fluctuations, and rotations of their structural planes. These observations suggest that DNA recognition and binding by small molecules may be governed by mechanism(s) that are much more complex than initially anticipated and may represent unexpected challenges in genome-targeted drug design.
人类基因组序列的知识为在合理设计治疗药物时将DNA作为靶点提供了重要机遇。在靶向DNA的药物中,纺锤菌素对富含A/T的区域表现出强烈的结合偏好。为了研究负责纺锤菌素识别和结合DNA的关键因素,对一种DNA-纺锤菌素复合物进行了分子动力学模拟,其中两个纺锤菌素分子与16聚体d(CTTAATTCGAATTAAG)(2)的每个AATT位点结合。在这个复合物中,两个纺锤菌素以头对头的方向结合在DNA小沟中,两个纺锤菌素的胍基末端都指向DNA的中心。尽管它们的环境相同,但分子动力学模拟表明,两个纺锤菌素在各自的均方根行为、结合能、小沟宽度波动以及结构平面的旋转方面存在差异。这些观察结果表明,小分子对DNA的识别和结合可能受比最初预期更为复杂的机制所支配,并且可能在基因组靶向药物设计中带来意想不到的挑战。