About this Research Topic
Higher organisms, starting from a limited number of genes, expand the functionalities of proteins through post-translational modification. In this way, the diversity of protein structures and functions can be tremendously increased. Protein modifications also occur in pathological conditions, such as carbonylation due to oxidative stress or glycation leading to advanced glycation end products (AGEs), observed as a result of aging and degenerative diseases. Drawing inspiration from nature, the chemical modification of proteins and oligopeptides is an important tool in many different applications, including the development of new therapies, diagnostic devices, and analytic systems.
Historically, chemical reactions developed for small molecules were aimed at obtaining a unique product, and did not focus on tri-dimensional structural integrity or the various reactivities potentially displayed by the reactant. Hence, proteins and oligopeptides for site-selective modifications require precise control over chemo- and regioselectivity, as well as mild operating conditions to obtain a final adduct carrying the desired chemical modifications on a functionally competent biological molecule.
The development of new protocols and the comprehension of functionalization mechanisms represent important challenges in chemical biology, biopharmaceutics, biosensor development, and materials science. In this Research Topic, we aim to collect contributions covering all aspects of protein and oligopeptide chemical modification, from synthesis to characterization and applications.
Areas to be covered in this Research Topic may include, but are not limited to:
• Protein chemical modification in biopharmaceuticals (e.g. enzyme and antibody PEGylation, insertion of non-standard amino acids)
• Mechanistic and biological activity study of ribosomally synthesized and post-translationally modified peptides (RiPP)
• Protein and oligopeptide labeling for in vitro biosensing and in vivo imaging
• Chemical modifications for bio-orthogonal and pre-targeted chemistry
• Protein target chemical modification for analytical applications
• Probing and characterization of biological systems
Historically, chemical reactions developed for small molecules were aimed at obtaining a unique product, and did not focus on tri-dimensional structural integrity or the various reactivities potentially displayed by the reactant. Hence, proteins and oligopeptides for site-selective modifications require precise control over chemo- and regioselectivity, as well as mild operating conditions to obtain a final adduct carrying the desired chemical modifications on a functionally competent biological molecule.
The development of new protocols and the comprehension of functionalization mechanisms represent important challenges in chemical biology, biopharmaceutics, biosensor development, and materials science. In this Research Topic, we aim to collect contributions covering all aspects of protein and oligopeptide chemical modification, from synthesis to characterization and applications.
Areas to be covered in this Research Topic may include, but are not limited to:
• Protein chemical modification in biopharmaceuticals (e.g. enzyme and antibody PEGylation, insertion of non-standard amino acids)
• Mechanistic and biological activity study of ribosomally synthesized and post-translationally modified peptides (RiPP)
• Protein and oligopeptide labeling for in vitro biosensing and in vivo imaging
• Chemical modifications for bio-orthogonal and pre-targeted chemistry
• Protein target chemical modification for analytical applications
• Probing and characterization of biological systems
Keywords: post-translational modifications, bioconjugation, labeling, biopharmaceuticals, non-standard amino acids
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.
