Developing probes of cathepsin L - Lab Report Example

The resin has a linker of acid sensitivity that allows the protection of dipeptide. Besides, the cleavage process also affects the selection of the resin. The synthesis process involved adopting the SPPS protocol which involves the use of DMF, resin, reagents like 4-Dimethylamionpyridine (DMAP) and DMF before the addition of liquid reagent (DIC). The resins were washed with DCM3, IPO 3 and NMP 3 several times. The cleavage process involves using a dilute TFA process. The dry resin was placed in the glass funnel and 1% 10 ml FTA of the dry DCM added, filtered through the application of nitrogen pressure on the flask with ten percent pyridine (2ml) dissolved in methanol.

The washing of resin and checking of the filtrate using either the HPLC or the TLC method helped in the process. The mass spectrometry was used for the identification of the protein profiles. The mass of the protein were evaluated by the calculation of m/z peaks. The cleavage of the protein was successful and lead to the identification of 12 peaks. Majority of the cathepsins are cysteine protease while others are either serine or aspartic proteases. The secretion of cathepsins in the body can be induced by factors like interferon and tumour necrosis factor (Hassanein et al., 2009). Different cathepsins are induced by different molecules, for instance cathepsin L is induced by nicotine.

Cathepsins are proteases. Proteases are enzymes with the potential to degrading the proteins. These enzymes are ubiquitous in animals and other organisms. The cathepsins occur in different forms and families. Their differences are based on the differences in structural domains (Puzer et al., 2005). Other factors affecting the type of cathepsins include the proteins they cleave and the catalytic mechanisms. The optimal environment for these enzymes is acidic media, therefore, most of the cathepsins undergo activation at lower ionic concentration characterised by the