Methods and Results: A range of DH % (50-100) of PKE peptides was prepared using alcalase, and hydrolysis conditions were determined using response surface methodology (RSM). The influence of pH (6.5-10.5), temperature (35-65 degrees C), enzyme/substrate E7080 molecular weight ratio (1-5%) and substrate concentration (1-2%) were studied on the response of the DH. The antibacterial activity of different DH % of PKE peptides was tested by using disc diffusion assay and micro-broth dilution assay. According to the minimum inhibitory
concentration (MIC) test on each of the PKE peptides of different DH %, the 70 DH % PKE peptide showed greater inhibitory effect compared to the 100 DH % PKE peptide against B. cereus, B. coagulans, B. megaterium, B. pumilus, B. stearothermophillus, B. subtilis, B. thuringiensis, Cl. perfringens, Lisinibacillus sphaericus and L. monocytogenes.
Conclusions: The 70 DH % PKE peptides exhibited greatest overall antibacterial effect of the various peptides of PKE evaluated. Further research is needed to determine the mode of action of PKE peptides.
Significance Idasanutlin supplier and Impact of the Study: Palm kernel expeller peptides, a natural plant
product, effectively inhibited the growth of spore-forming and non-spore-forming Gram-positive bacteria. Potentially, PKE peptides could be used in food preservation and developed as antibacterial agent in the pharmaceutical industry.”
“Matrix metalloproteinases (MMPs) have been almost exclusively thought to be secreted proteases (with the exception of the membrane-type MMPs) that exert diverse biological actions in health and disease via proteolyzing substrates outside the cell. However, recent evidence has demonstrated that the role of MMPs
goes far beyond their proteolytic activity in the extracellular matrix. MMP-2 is arguably the most ubiquitous member of the 23 member MMP family and is expressed in all cells of the heart and vasculature. In the past 10 years, MMP-2 was shown to change the bioactivity of a growing list of specific, non-extracellular matrix proteins both outside and inside the cell. There is clear evidence of its intracellular localization to the cardiac sarcomere, nucleus, and mitochondria and that during early phases of Flavopiridol oxidative stress injury to the heart, MMP-2 proteolyzes specific sarcomeric and cytoskeletal proteins to cause contractile dysfunction. In this review we discuss this novel intracellular biology of MMP-2 and the potential use of MMP inhibitors for the therapy of heart injury caused by oxidative stress. (Trends Cardiovasc Med 2011;21:112-118) (C) 2011 Elsevier Inc. All rights reserved.”
“Background: The neural cell adhesion molecule 1(NCAM1, aliases NCAM and CD56) is a cell-surface molecule which makes homophilic adhesion between neural cells involved in cell migration, axon outgrowth and synaptic plasticity.