Infectious diseases are caused by bacteria, fungus, viruses, and other microorganisms. Biomolecules such as proteins, DNA, and/or RNA play a crucial role in the infections of these disorders. These infectious illnesses are often transmissible, meaning they may be passed from one person to another by a variety of means. Even though medical technology has progressed, some illnesses continue to cause anxiety among individuals worldwide. If we examine the situation of COVID-19, the entire world is terrified of the pandemic. Similarly, In the last decades, other infections including Dengue, Chikungunya, Zika, Ebola, Japanese Encephalitis Virus (JEV), influenza, the common cold, tuberculosis (TB), Hepatitis A and B and human immunodeficiency syndrome (HIV) have also challenged the human population.
Advanced state-of-the-art computational and experimental methods have radically altered the medical sciences, allowing researchers to explore therapies for any ailment in a relatively short amount of time. Computer simulation aids in the discovery of mechanistic insights into proteins, protein ligands, protein-protein, protein-DNA, and other biomolecular interactions. MD simulation not only aids in understanding the system's physical processes at the atomic level, but also allows for the discovery of hidden states that are not detectable empirically. Additionally, experimental measurements of the thermodynamic properties in biomolecular systems are often costly and time-consuming. Accurate theoretical calculations of their free energies via numerical simulation are becoming increasingly important in a variety of fields, including rational drug design, protein folding, and protein–protein interactions (PPIs), among others. PPIs are involved in nearly all biological activities in a living cell, and a number of PPIs have been proposed as therapeutic targets. A protein–protein complex's 3D structure can reveal the broad breadth of how and where one protein interacts with another. Nowadays, a range of experimental approaches have been developed to investigate whether two proteins interact. However, without comprehensive structural knowledge, it is difficult to understand how two proteins interact using conventional biophysical and/or biochemical approaches. X-ray crystallography, cryogenic electron microscopy (cryo-EM), and nuclear magnetic resonance (NMR) methods may identify the native structure of a protein monomer or a protein–protein complex at the atomic level, notwithstanding their limitations. But it is a very difficult, or impossible, task to solve the high-resolutions structures for all PPI. So, in this case, a combination of computational and experimental methods are important to explain the interactions between two proteins in a complex.
There are several types of therapeutics available for the treatment of these diseases. However, resistance to many antibiotics and immune escape from vaccines suggests an utmost need for the design and development of novel therapeutics (such as small inhibitors, peptide inhibitors, biomimetics, vaccines etc.). Moreover, novel therapeutic strategies and delivery systems targeting the pathogen, host factors, and evaluating their mode of action, need more attention.
The Guest Editors invites authors to publish original research articles, short communication, perspectives, methods, and reviews, and aim to bring together a collection of articles highlighting, but not limited to: Design and development of therapeutics (small inhibitors, peptide inhibitors, biomimetics, vaccines etc.) against infectious diseases using computational and/or experimental approaches
Infectious diseases are caused by bacteria, fungus, viruses, and other microorganisms. Biomolecules such as proteins, DNA, and/or RNA play a crucial role in the infections of these disorders. These infectious illnesses are often transmissible, meaning they may be passed from one person to another by a variety of means. Even though medical technology has progressed, some illnesses continue to cause anxiety among individuals worldwide. If we examine the situation of COVID-19, the entire world is terrified of the pandemic. Similarly, In the last decades, other infections including Dengue, Chikungunya, Zika, Ebola, Japanese Encephalitis Virus (JEV), influenza, the common cold, tuberculosis (TB), Hepatitis A and B and human immunodeficiency syndrome (HIV) have also challenged the human population.
Advanced state-of-the-art computational and experimental methods have radically altered the medical sciences, allowing researchers to explore therapies for any ailment in a relatively short amount of time. Computer simulation aids in the discovery of mechanistic insights into proteins, protein ligands, protein-protein, protein-DNA, and other biomolecular interactions. MD simulation not only aids in understanding the system's physical processes at the atomic level, but also allows for the discovery of hidden states that are not detectable empirically. Additionally, experimental measurements of the thermodynamic properties in biomolecular systems are often costly and time-consuming. Accurate theoretical calculations of their free energies via numerical simulation are becoming increasingly important in a variety of fields, including rational drug design, protein folding, and protein–protein interactions (PPIs), among others. PPIs are involved in nearly all biological activities in a living cell, and a number of PPIs have been proposed as therapeutic targets. A protein–protein complex's 3D structure can reveal the broad breadth of how and where one protein interacts with another. Nowadays, a range of experimental approaches have been developed to investigate whether two proteins interact. However, without comprehensive structural knowledge, it is difficult to understand how two proteins interact using conventional biophysical and/or biochemical approaches. X-ray crystallography, cryogenic electron microscopy (cryo-EM), and nuclear magnetic resonance (NMR) methods may identify the native structure of a protein monomer or a protein–protein complex at the atomic level, notwithstanding their limitations. But it is a very difficult, or impossible, task to solve the high-resolutions structures for all PPI. So, in this case, a combination of computational and experimental methods are important to explain the interactions between two proteins in a complex.
There are several types of therapeutics available for the treatment of these diseases. However, resistance to many antibiotics and immune escape from vaccines suggests an utmost need for the design and development of novel therapeutics (such as small inhibitors, peptide inhibitors, biomimetics, vaccines etc.). Moreover, novel therapeutic strategies and delivery systems targeting the pathogen, host factors, and evaluating their mode of action, need more attention.
The Guest Editors invites authors to publish original research articles, short communication, perspectives, methods, and reviews, and aim to bring together a collection of articles highlighting, but not limited to: Design and development of therapeutics (small inhibitors, peptide inhibitors, biomimetics, vaccines etc.) against infectious diseases using computational and/or experimental approaches