Protein structuromics: New observations for translational medicine research in lung cance

Abstract

Abstract Lung cancer, also known as lung carcinoma, is a malignant tumour of the lung caused by genetic damage to the DNA of airway cells, often exacerbated by cigarette smoking or inhalation of damaging chemicals. Despite advances in molecular biology and treatment, there are still many questions that need to be answered regarding lung cancer occurrence and the underlying mechanism. In this study, we assessed the protein structural features of 20 oncogene-related and 20 anti-oncogene-related proteins via protein sequences, folding rate, structural and dynamic analysis methods. Our results directly indicated that oncogene-related group proteins show more stable-complex structures than anti-oncogene-related group proteins. When a tumour occurs or different treatments are administered, cell microenvironment changes in the lungs are always more complex than the normal situation. Additionally, oncogene-related proteins comprise more kinds of packet-type proteins than anti-oncogene-related proteins. Even if the structures of the two groups of proteins are disrupted, more unfavourable group proteins persist and refold faster to achieve their correct shape and perform their functions more quickly than favourable group proteins; thus, the former support cancer development. We hope that these analyses will contribute to the understanding of the developmental mechanism of lung cancer and inform the design of new treatments.