One of the major reasons for studying chemical kinetics is to use measurements of the macroscopic properties of a system, Safety of Hemin, such as the rate of change in the concentration of reactants or products with time.In a article, mentioned the application of 16009-13-5, Name is Hemin, molecular formula is C34H32ClFeN4O4
Hemin and bile pigments are the secondary structure regulators of intrinsically disordered antimicrobial peptides
The interaction of protoporphyrin compounds of human origin with the major bee venom component melittin (26 a.a., Z +6) and its hybrid derivative (CM15, 15 a.a., Z +6) were studied by a combination of various spectroscopic methods. Throughout a two-state, concentration-dependent process, hemin and its metabolites (biliverdin, bilirubin, bilirubin ditaurate) increase the parallel beta-sheet content of the natively unfolded melittin, suggesting the oligomerization of the peptide chains. In contrast, alpha-helix promoting effect was observed with the also disordered but more cationic CM15. According to fluorescence quenching experiments, the sole Trp residue of melittin is the key player during the binding, in the vicinity of which the first pigment molecule is accommodated presumably making indole-porphyrin pi-pi stacking interaction. As circular dichroism titration data suggest, cooperative association of additional ligands subsequently occurs, resulting in multimeric complexes with an apparent dissociation constant ranged from 20 to 65?muM. Spectroscopic measurements conducted with the bilirubin catabolite urobilin and stercobilin refer to the requirement of intact dipyrrinone moieties for inducing secondary structure transformations. The binding topography of porphyrin rings on a model parallel beta-sheet motif was evaluated by absorption spectroscopy and computational modeling showing a slipped-cofacial binding mode responsible for the red shift and hypochromism of the Soret band. Our results may aid to recognize porphyrin-responsive binding motifs of biologically relevant, intrinsically disordered peptides and proteins, where transient conformations play a vital role in their functions.
Hemin and bile pigments are the secondary structure regulators of intrinsically disordered antimicrobial peptides
Sometimes chemists are able to propose two or more mechanisms that are consistent with the available data. Safety of Hemin, If a proposed mechanism predicts the wrong experimental rate law, however, the mechanism must be incorrect.Welcome to check out more blogs about 16009-13-5, in my other articles.
Reference£º
Iron Catalysis in Organic Synthesis | Chemical Reviews,
Iron Catalysis in Organic Synthesis: A Critical Assessment of What It Takes To Make This Base Metal a Multitasking Champion