Peptide-Fe complexes have been identified as promising iron-chelators, and peptide segments that change their conformation due to external stimuli have been used in peptide-based molecular devices. Additionally, experiments modeling volcanic or hydrothermal settings have shown that amino acids can be converted into their peptides by use of coprecipitated (Ni,Fe)S and CO. Finally, an Integrated Peptide and Protein prediction Framework based on Fused features and Ensemble models (IPPF-FE) has been proposed to precisely predict peptides.
Peptide-Fe complexes are formed mainly through the carboxyl and hydroxyl oxygen bond. Different metal ligands have been used to synthesize peptide-iron complexes, which have properties such as containing 5.6% Fe and potential to reduce undesirable sensory changes in food products. Gas phase studies of metal-peptide complexes can help understand intrinsic properties of the complex, such as 2H + Fe]+ ions.
Peptide-Fe complexes are generally stable, with studies showing that they can maintain their structural and physical-chemical stability over 1 year of storage. The peptide-zinc complex has also been shown to enhance the stability of zinc during in vitro gastrointestinal digestion. Additionally, a strong ionic signal corresponding to a FeIII complex was observed with LSIMS in the positive ion mode.