Metallopeptides
A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".
Deadline for manuscript submissions: closed (20 June 2017) | Viewed by 40934
Special Issue Editor
Interests: supramolecular chemistry; chemical biology; coordination chemistry; self-assembly; biosensing; biolabeling; molecular devices and machines; DNA-binding; theranostic drugs; peptides and metallopeptides; helicates
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Special Issue Information
Dear Colleagues,
Metalloproteins can be defined as those proteins that contain at least one metal ion in their structure. Diverse studies estimate that about one third of all proteins need of metal ions to correctly perform their functions, including catalysis, transport, signal transduction, storage, detoxification or DNA transcription, among others. Over the last thirty years, many groups have focused their research efforts in understand the structural, folding and functional aspects of metalloproteins, and applying this knowledge to the design of new systems with novel and improved structural, spectroscopic, biological or catalytic properties. However, the large size of most metalloproteins requires their production by in vitro expression, so that the introduction of extrinsic functionalities typically requires cumbersome protocols, or postsynthetic modifications, which typically suffer from poor selectivity.
On the other hand, metallopeptides encode in their amino acid sequence precise structural and functional information, and represent excellent model systems that can be used as simplified mimetics of metalloproteins. In contrast with them, metallopeptides can be easily synthesized, modified and functionalized through chemical means, and can be easily and quickly produced in large quantities. Therefore, the scientific interest of the synthetic, structural and folding aspects of metallopeptides, as well as their functional application in a variety of areas has exponentially increased in the last few years.
Furthermore, the metallopeptides are not limited to systems built with the set of twenty natural amino acids, and allow the straightforward incorporation in their sequence of unnatural coordinating amino acids equipped with chelating ligands, such as 2,2′-bipyridine or 2,2′:6′,2′′-terpyridine, which greatly simplify the creation of appropriate coordinating environments and the definition of the microarchitecture of the peptide ligands to create artificial metal-peptide hybrids that potentially combine the functional versatility of metal complexes with the biological properties of peptide systems.
This Special Issue of Molecules wants to highlight this multidisciplinary scientific subject of increasing interest and enormous potential. Original research, as well as review papers dealing with all aspects of natural and unnatural metallopeptides, including synthesis, structural and folding properties and functional applications in catalysis, metal storage, metal transport, metal detoxification, DNA-binding, biosensing, biolabeling, etc., or as antibacterial/cytotoxic drugs, molecular machines, etc., are welcome for inclusion in this Special Issue of Molecules.
Prof. Miguel Vázquez López
Guest Editor
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Keywords
- metallopeptide synthesis
- structural aspects
- folding of metallopeptides
- DNA-binding
- catalysis
- biosensing
- bioconjugation
- molecular machines
- metal detoxification
- transport and storage
- theranostic drugs
- ionophores
- chemical biology
- supramolecular chemistry
- medicinal chemistry and biomaterials
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