About this Research Topic
Nature has provided a plethora of highly potent bioactive peptides and miniproteins that contain multiple disulfide bonds which form the basis of the molecule’s conformation. Such disulfide-rich peptides and miniproteins are found in the venoms, plants, and microbes. The distinct cysteine pattern and disulfide connectivity result in a specific structural conformation, responsible for the biological activity at a variety of targets. As these natural compounds target many crucial enzymes, receptors and ion channels, they represent promising candidates for the design of novel research tools and therapeutics for biomedical applications.
However, one drawback is the challenging synthesis and unambiguous analytical characterization of the peptides owing to the complexity of the oxidative folding procedure which may lead to the concomitant occurrence of conformational disulfide isomers. Consequently, several efforts have been undertaken to facilitate the synthesis of promising disulfide-rich peptides. These include, disulfide bridge substitution/removal or the optimization of oxidation procedures. In terms of accurate characterization of disulfide-rich peptides, analytical methods such as HPLC, mass spectrometry and NMR have been proven as indispensable.
This Research Topic focuses on the specific challenges related to the chemical production of disulfide-rich peptides and miniproteins along with the associated difficulties of their chemical and structural analysis by mass spectrometry and NMR spectroscopy.
Areas to be covered in this Research Topic may include, but are not limited to:
- Chemical synthesis of disulfide-rich peptides and miniproteins
- Optimization of oxidation procedures
- Disulfide-rich peptides and miniprotein characterization
- Novel characterization techniques
- Tools and methods for the analysis of disulfide-rich peptides
- Synthesis and biomedical applications of disulfide-rich peptides
- Machine learning methods for disulfide-rich peptides and miniprotein synthesis and characterization
- Molecular modeling, docking and molecular dynamics relating to experimental data on peptide activity, target binding and structural information
However, one drawback is the challenging synthesis and unambiguous analytical characterization of the peptides owing to the complexity of the oxidative folding procedure which may lead to the concomitant occurrence of conformational disulfide isomers. Consequently, several efforts have been undertaken to facilitate the synthesis of promising disulfide-rich peptides. These include, disulfide bridge substitution/removal or the optimization of oxidation procedures. In terms of accurate characterization of disulfide-rich peptides, analytical methods such as HPLC, mass spectrometry and NMR have been proven as indispensable.
This Research Topic focuses on the specific challenges related to the chemical production of disulfide-rich peptides and miniproteins along with the associated difficulties of their chemical and structural analysis by mass spectrometry and NMR spectroscopy.
Areas to be covered in this Research Topic may include, but are not limited to:
- Chemical synthesis of disulfide-rich peptides and miniproteins
- Optimization of oxidation procedures
- Disulfide-rich peptides and miniprotein characterization
- Novel characterization techniques
- Tools and methods for the analysis of disulfide-rich peptides
- Synthesis and biomedical applications of disulfide-rich peptides
- Machine learning methods for disulfide-rich peptides and miniprotein synthesis and characterization
- Molecular modeling, docking and molecular dynamics relating to experimental data on peptide activity, target binding and structural information
Keywords: Cysteine-rich peptides/proteins, disulfide bonds, synthesis and folding, structure analysis, structure-activity relationships
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