Spectroscopic method for estimation of MMP-9 enzyme concentration and activity

Add time:08/15/2019    Source:sciencedirect.com

Two highly sensitive fluorescent dye-labelled peptide indicators for metalloproteinase 9 (MMP-9) activity were designed and tested in vitro. Excellent sensitivity of these indicators is achieved by careful selection of the amino acid sequence corresponding to the substrate recognition preference of MMP-9. The phenomenon of Förster resonance energy transfer (FRET) is applied for detection of the peptide cleavage by MMP-9. FRET occurs between fluorescent dyes AMCA (donor) and TAMRA (acceptor) bound to the flexible peptide fragments differing in the donor acceptor separation distance. Enzymatic hydrolysis of the peptide leads to a significant weakening of energy transfer and increased donor fluorescence intensity. The enzyme action efficiency is higher for the longer proline-rich peptide which is reflected in the results of steady-state fluorescence studies. In particular, the use of longer peptide allows shorter detection time of MMP-9 (about 20–30 min). The possible reasons for this effect are discussed.

We also recommend Trading Suppliers and Manufacturers of 9(S)-HETE (cas 107656-13-3). Pls Click Website Link as below: cas 107656-13-3 suppliers

Prev:Membrane-related oxysterol function: preliminary results on the modification of protein kinase C activity and substrate phosphorylation by 7ß,25-dihydroxycholesterol
Next:Production of R,R-2,3-butanediol of ultra-high optical purity from Paenibacillus polymyxa ZJ-9 using homologous recombination)