76046-35-0Relevant articles and documents
A new family of highly potent inhibitors of microbes: Synthesis and conjugation of elastin based peptides to piperazine derivative
Suhas,Chandrashekar,Gowda, D. Channe
experimental part, p. 89 - 98 (2012/09/05)
Elastin protein-based polymers have their origin in repeating sequences of the mammalian elastic protein, elastin. The sequences of elastin peptides chosen are tetrapeptides, pentapeptides and tricosamers (30 amino acids) and also aromatic amino acids. Th
Hydrophobicity Dependence of Oxidation of Tetrapeptides of Elastin Sequences with Mn(III): Synthesis, Characterization, Kinetics, and Mechanistic Study
Kempe Gowda, B. K.,Prasad, H. S.,Rangappa, K. S.,Channe Gowda, D.
, p. 39 - 48 (2007/10/03)
The analogues of elastin sequences, glycyl-glycyl-alanyl-proline (GGAP), glycyl-glycyl-phenylalanyl-proline (GGFP), and glycyl-glycyl-isoleucyl-proline (GGIP) were synthesized by classical solution phase method and characterized. The kinetics of oxidation of these tetrapeptides (TETP) by Mn(III) has been studied in the presence of sulphate ions in acidic solution at 25 deg C. The reaction was followed spectrophotometrically at λmax = 500 nm. A first-order dependence of rate on both [Mn(III)] and [TETP] was observed. The rate is independent of the concentration of the reduction product, Mn(II), and hydrogen ions. The effects of varying the dielectric constant of the medium and addition of anions such as sulphate, chloride, or perchlorate were studied. Activation parameters have been evaluated using Arrhenius and Eyring plots. The oxidation products were isolated and characterized. A mechanism involving the reaction of TETP with Mn(III) in the rate-limiting step is suggested. An apparent correlation was noted between the rate of oxidation and the hydrophobicity of these sequences, where increased hydrophobicity results in increased rate of oxidation.
