Today's blog post is much later than usual due to ongoing consulting commitments, but when an alert flashed up on my email with the above header, I couldn't resist taking a break and reading it:
Wow, that got my attention. Here's a link to the letter published in Nature.
What does this mean in practise? Well, put simply once we know the precise structure of the target enzyme, new generation aromatase inhibitors can be developed to improve on the effectiveness and tolerability of existing inhibitors such as Femara, Arimidex and Aromasin.
Or as the lead researcher Dr Ghosh more enthusiastically put it:
"Scientists worldwide have been trying for 35 years to crystallize this membrane-bound enzyme and we are the first to succeed. Now that we know the structures of all three key enzymes implicated in estrogen-dependant breast cancers, our goal is to have a personalized cocktail of inhibitors customized to the specific treatment needs of each patient. Our knowledge about these three enzymes will enable us to develop three mutually exclusive inhibitors customized to each patient's needs which will work in harmony together with minimal side effects."
It is important to note that 70-80% of breast cancers are fed by the female hormones estrogen (ER+) or progesterone (PR+), so inhibiting the hormones can slow down cancer growth. Current methods of doing so include treatment with tamoxifen or the first-generation aromatase inhibitors, but knowing the structure of both is crucial to designing better drugs in the future in order to minimise drug resistance and relapse.