A mechanical, in vitro study of saffron carotenoids (crocin) function.

What is it about?

This paper reports the new finding of crocin binding to Albumin, using different in vitro and ex vivo techniques. This is the first time that crocin-Albumin interaction is investigated. We found that the carotenoid backbone of crocin binds to the hydrophobic site in Albumin; but, two gentiobiosyl residues prevent its complete penetration into the site. These groups bind through hydrogen binding. This interaction affects the environment of only Trp residue of Albumin and quenches its fluorescence emission.

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Why is it important?

The only difference between crocin and crocetin is the gentiobiosyl residues that affect the function, in the term of protein binding. It is an important finding in the field of Structure-Function Relationship.