The Role of Structural Bioinformatics in Understanding Tumor Necrosis Factor α-Interacting Protein Mechanisms in Chronic Inflammatory Diseases: A Review

Author:

Bastos Luana Luiza1,Mariano Diego1ORCID,Lemos Rafael Pereira1,Bialves Tatiane Senna1,Oliveira Carlo Jose Freire2,de Melo-Minardi Raquel C.1ORCID

Affiliation:

1. Laboratory of Bioinformatics and Systems, Department of Computer Science, Institute of Exact Sciences, Universidade Federal de Minas Gerais, Belo Horizonte 31270-901, Brazil

2. Laboratory of Immunology and Bioinformatics, Institute of Natural and Biological Sciences, Federal University of Triângulo Mineiro, Uberaba 38025-180, Brazil

Abstract

Tumor necrosis factor α (TNF-α) is a multifunctional cytokine protein acknowledged as a vital mediator in cell differentiation, proliferation, and survival. Additionally, TNF-α is a crucial component of the host’s defense by mediating inflammatory and immune responses against various aggressive agents, including viruses, bacteria parasites, and tumors. However, excessive production can be detrimental to the body and is also implicated in developing several inflammatory and immune-mediated disorders. Therefore, there is great interest in studying its role and its modulation, in various diseases, both in in vitro, in vivo, and in silico experiments. In this review, we evaluated the structures of proteins related to TNF-α available in public databases. In addition, we described the main antibodies blocking this cytokine and its applications and commented on the potential of naturally produced binding molecules, such as TNF-α-binding proteins produced by ticks. We also discuss the role of structural bioinformatics techniques in understanding the mechanisms of chronic inflammatory diseases related to TNF-α. We hope that the data presented in this review will be useful for studies that aim to better understand the mechanisms of the interactions of TNF-α with other proteins and will lead to new drugs or treatments.

Funder

CAPES

CNPq

FAPEMIG

Publisher

MDPI AG

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