After greetings.
I have a question for the specialists.
Given the ongoing scientific debate surrounding the biochemical role of vitamin B17 (amygdalin) in cancer treatment, what is the most reliable and practical laboratory approach to accurately differentiate between the molecular structure of amygdalin in its stable, inactive state and its potentially active form when exposed to cancerous cells? Specifically, which analytical techniques such as NMR spectroscopy, mass spectrometry, or chromatography are best suited to detect and characterize any structural or conformational changes in amygdalin under these biological conditions, and how can such distinctions contribute to a clearer understanding of its pharmacological activity?
Many thanks and respect to those who helped answer my query.
Amygdalin is a kind of small molecule and can be characterized using NMR and mass spec in combination after a proper purification strategy has been implemented. Column chromatography, preparative LC can be used to isolate the amygdalin.
I do not expect it to be inactivated by any inducing a conformational change. If it interacts with a partner, co-purifying it with its conjugate (e.g., Co-IP) would be beneficial to say something about its efficacy.
Free amygdalin isolation and characterizing its structure (resolving spatial isomers if there are any) might not be clarifying for this purpose if its efficacy is linked to its conformational behavior, rather than chiral purification is needed after total amygdalin isolation.
The nitrile part of the molecule may also be useful to chemically couple or to find a more unique resin in isolating the compound.
However, as I mentioned, it would be better to test its interacting partners to elucidate its activity pattern. In this scenario, you will need an immunoaffinity isolation (anti-amygdalin antibody) to fish out the amygdalin and amygdalin-bound compounds (proteins, oligonucleotides, enzymes, etc)
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