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Alzheimers disease 1 Primary Source - FAD Mutations in Presenilin-1 or Amyloid Precursor Protein Decrease the Efficacy of a y-Secretase Inhibitor Evidence for Direct Involvement of PS1 in the y-Secretase Cleavage Complex Alzheimers disease AD causes mutations in presenilin-1 PS1 and presenilin -2 PS2 that increase the formation of amyloid B-peptides AB AB is formed by increasing the cleavage of B-amyloid precursor protein APP and the cleavage of APP is performed by y-secretase So in simpler terms AB peptides are formed by the cleavage of APP by B- and y- secretase In order to examine whether PS1 is directly involved in the y-secretase cleavage complex compound 1 was used to imitate the y-secretase cleavage region of APP which would inhibit the AB generating system This experiment proved that peptidomimetic inhibitors such as Compound 1 as well as aspartyl protease inhibitor pepstatin A could inhibit the activity of y-secretase which would decrease AB production and as a result there is a surplus of y-secretase substrates and this suggests that there is direct contact between the inhibitors and the active site of y-secretase It was found in this experiment that FAD familial Alzheimers disease causing mutations in APP or PS1 decreased the capacity of compound 1 to inhibit the cleavage of y-secretase The results of the experiment conclude that PS1 is directly involved in the cleavage of APP by y-secretase that results in the production of AB peptides This study showed that despite previous studies that claim that the increase of AB production is due to FAD that causes mutations in PS1 and PS2 the mechanism that causes this increased cleavage by y-secretase couldnt be determined This study also confirmed that 1 that their finding an optimal AB synthesis at a slightly acidic pH and 2 the inhibition of AB generation by the aspartyl protease inhibitor pepstatin A suggests that y-secretase is an aspartyl protease 2 Secondary Source - Enzyme offers promise of Alzheimers drugs The enzyme
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