2019年冠状病毒病(COVID-19)是一种新型疾病，对全球人类生活和国家经济产生了毁灭性影响。这种疾病表现出相似的寄生特性，需要宿主的生物分子来生存和繁殖。基于其结构，位于COVID-19病毒表面的刺突糖蛋白严重急性呼吸综合征冠状病毒2（SARS-CoV-2刺突蛋白）是抗病毒药物开发的潜在热点。COVID-19病毒使协助攻击者的伴侣系统采取行动，因此有利于感染。为了研究SARS-CoV-2刺突蛋白与人类分子伴侣（HSPA8和sHSP27）之间的相互作用，进行了一系列步骤，包括序列获得和分析，然后是多个序列比对，同源建模，和蛋白质-蛋白质对接，我们使用Cluspro进行预测SARS-CoV-2刺突蛋白与感兴趣的人类分子伴侣之间的相互作用。我们的发现描述了SARS-CoV-2刺突蛋白由三条不同的链组成，链条A,B,C,它们相互作用形成氢键，疏水相互作用，以及与人HSPA8和HSP27的静电相互作用，其中-828.3和-827.9kcal/mol作为人HSPA8和-1166.7和-1165.9kcal/mol的结合能。
Coronavirus disease 2019 (COVID-19) is a novel disease that had devastating effects on human lives and the country\'s economies worldwide. This disease shows similar parasitic traits, requiring the host\'s biomolecules for its survival and propagation. Spike glycoproteins severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2 spike protein) located on the surface of the COVID-19 virus serve as a potential hotspot for antiviral drug development based on their structure. COVID-19 virus calls into action the chaperonin system that assists the attacker, hence favoring infection. To investigate the interaction that occurs between SARS-CoV-2 spike protein and human molecular chaperons (HSPA8 and sHSP27), a series of steps were carried out which included sequence attainment and analysis, followed by multiple sequence alignment, homology modeling, and protein-protein docking which we performed using Cluspro to predict the interactions between SARS-CoV-2 spike protein and human molecular chaperones of interest. Our findings depicted that SARS-CoV-2 spike protein consists of three distinct chains, chains A, B, and C, which interact forming hydrogen bonds, hydrophobic interactions, and electrostatic interactions with both human HSPA8 and HSP27 with -828.3 and -827.9 kcal/mol as binding energies for human HSPA8 and -1166.7 and -1165.9 kcal/mol for HSP27.
