Elective Affinities
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".
Deadline for manuscript submissions: closed (20 February 2025) | Viewed by 2690
Special Issue Editors
Interests: re-entrant phase transitions; protein–ligand and protein–protein interactions; protein folding, misfolding and aggregation; glycoproteins; isotopically labeled recombinant protein expression and purification; spectroscopy methods; molecular docking and molecular dynamics
Interests: protein–ligand and protein–protein interactions; protein folding, misfolding, and aggregation; antiviral lectins; gold nanoparticles; isotopically labeled recombinant protein expression and purification; nuclear magnetic resonance spectroscopy; X-ray protein crystallography
Special Issue Information
Dear Colleagues,
Affinity, a complex trait or behaviour noticeable “at first sight” or that develops over time due to a particular reason or tendency, plays an important role in social, biological, and chemical environments. In 1809, the great poet, novelist, statesman, and scientist Johann Wolfgang von Goethe was surprised by the similarities between these rather different fields in his third critically acclaimed and influential novel, Die Wahlverwandtschaften. Our world is built on dynamic processes of attraction and repulsion, which have drastic consequences. Curiously, affinity does not always lead to good outcomes, and what we all know is that it is quite difficult to be controlled or influenced.
At the atomic and molecular levels, the types of interactions which shape the quantum world are extremely diverse. Affinity drives chemical reactions and influences how molecules interact. A simple molecule, such as water, has and mediates so many complex behaviors, never ceasing to surprise us. Water is the main constituent of Earth's hygrosphpere and is vital for all forms of life. A particularly relevant example is that the re-entrant phase transitions in simple hydrogen-bonded systems manifest through a closed-loop immiscibility gap or can drive dynamic substructure droplet formation. Even more, they can turn into rather unusual, reversible, liquid-to-solid phase transitions upon heating (J. Chem. Phys. (2004) 121(11), 5031). Somehow related, liquid–liquid phase transitions have also emerged as a fascinating area of research, providing new insights into the formation of biomolecular condensates and membrane-less organelles, which allow for the spatial organization and compartmentalization of cellular components. If we add here the complexity of protein–protein, protein–DNA, and protein–RNA interactions, we can understand the vastness of systems where selective affinities play a significant role. The dysregulation of these interactions can possibly lead to protein misfolding and aggregation, which are associated with a wide range of diseases, such as neurodegenerative disorders and cataracts. Additionally, we also remember that viruses trick the immune system into escaping antiviral defenses and adapting to easily penetrate and infect cells, which allows them to replicate and spread to new hosts. Post-translational modifications, such as glycosylation, are additionally important here, and glycobiology is also a remarkable field of research. In the same area, antibody production after the natural immune response is time-consuming, costly, and limits feasible targets. Understanding the underlying molecular mechanisms of all these improved affinities and finding ways to modulate them are crucial for developing effective therapeutic strategies.
This Special Issue aims to explore the latest advancements in this vast field of research. Even if we are actually particularly focused on protein–protein interactions, misfolding, and aggregation, in the context of cataracts—a leading cause of visual impairment and blindness worldwide which is characterized by the accumulation of protein aggregates within the eye lens—we are open to any original contribution analyzing molecular affinities experimentally (using physico-chemical and molecular biotechnology methods and spectroscopy) and theoretically (with the aid of modern computational methods, such as molecular docking and molecular dynamics) and ways to control their outcomes.We encourage researchers with diverse backgrounds, including (bio)physics, (bio)chemistry, structural biology, and molecular biotechnology, to contribute valuable insights to this issue.
Dr. Călin Gabriel Floare
Dr. Elena Matei
Guest Editors
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Keywords
- re-entrant and liquid-liquid phase transitions
- protein-ligand and protein-protein interactions
- protein folding, misfolding and aggregation
- chaperones
- spectroscopy methods
- structure-function relationship
- conformational transitions
- allostery
- molecular recognition
- molecular docking and molecular dynamics simulations
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