About this Research Topic
The exploding fields of biomedical research, biotechnology and, more recently, synthetic biology require the development of computational techniques paralleled by experimental methods to efficiently design novel materials inspired by living systems. Proteins immobilised on functionalised polymeric or biological surfaces are of particular importance as they are routinely being utilised in numerous biological measurements in laboratory and clinical settings.
A better understanding of the self-assembly of highly ordered peptide nanostructures is vital as not only does it help to uncover the pathogenesis of various neurodegenerative diseases but provides also new clues for a "bottom-up" design and fabrication of nanoscale devices and sensors for use in biomedicine. This broad range of applications emphasizes the importance of the nature of the substrate/interface, whether it be a cellular membrane or an inorganic solid surface, on the assembly of biomolecules, peptides and proteins, as these act as critical templates in many biological and nanotechnological processes. Interesting examples amongst many are: (a) The self-assembly of peptides on titanium interfaces have recently been shown to enhance biological conjugation of implants; (b) Immobilizing membrane proteins at interfaces for screening of pharmaceutical targets, characterising their structure and function and development of biosensors; (c) Label-free protein detection via self-assembly of protein-metallic nanoparticle structures; (d) Formation of patterned surfaces on solid substrates using self-assembled proteins.
One of the primary challenges that is faced when designing these nanoscale devices and sensors is the ability to tune the interface in order to optimise the self-assembly of the peptides near the device interface for the desired application. Therefore obtaining a molecular scale understanding of the interactions between peptides and the desired interface is of utmost importance. Computer simulations have proven to be a very powerful tool in providing insight into these interactions and therefore continue to play a significant part in the further development and design of these systems.
Due to the broad range of applications driven by this science, this field continues to become more and more interdisciplinary including medics, biologists, chemists, physicists, material scientists and engineers. Therefore, we encourage contributions to this Research Topic of Frontiers in Molecular Biosciences on this very exciting topic in which we will bring together the pre-eminent scientists in the various fields to discuss the open questions from the experimental and computational angles of attempting to gain a new level of understanding of the various roles that functionalised interfaces play in the aggregation of proteins.
A better understanding of the self-assembly of highly ordered peptide nanostructures is vital as not only does it help to uncover the pathogenesis of various neurodegenerative diseases but provides also new clues for a "bottom-up" design and fabrication of nanoscale devices and sensors for use in biomedicine. This broad range of applications emphasizes the importance of the nature of the substrate/interface, whether it be a cellular membrane or an inorganic solid surface, on the assembly of biomolecules, peptides and proteins, as these act as critical templates in many biological and nanotechnological processes. Interesting examples amongst many are: (a) The self-assembly of peptides on titanium interfaces have recently been shown to enhance biological conjugation of implants; (b) Immobilizing membrane proteins at interfaces for screening of pharmaceutical targets, characterising their structure and function and development of biosensors; (c) Label-free protein detection via self-assembly of protein-metallic nanoparticle structures; (d) Formation of patterned surfaces on solid substrates using self-assembled proteins.
One of the primary challenges that is faced when designing these nanoscale devices and sensors is the ability to tune the interface in order to optimise the self-assembly of the peptides near the device interface for the desired application. Therefore obtaining a molecular scale understanding of the interactions between peptides and the desired interface is of utmost importance. Computer simulations have proven to be a very powerful tool in providing insight into these interactions and therefore continue to play a significant part in the further development and design of these systems.
Due to the broad range of applications driven by this science, this field continues to become more and more interdisciplinary including medics, biologists, chemists, physicists, material scientists and engineers. Therefore, we encourage contributions to this Research Topic of Frontiers in Molecular Biosciences on this very exciting topic in which we will bring together the pre-eminent scientists in the various fields to discuss the open questions from the experimental and computational angles of attempting to gain a new level of understanding of the various roles that functionalised interfaces play in the aggregation of proteins.
Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.
