Com plexation of C۶۰ derivative as a carbo nic anhyd rase nan oscale enzyme inhibitor

Sever al carbonic a nhydrase (C A, EC ۴.۲. ۱.۱) isoforms, Figure ۱: A, are known to be present in the vertebrate central nervous system (C NS), being l ocated in various cell p opulations, where they play a var iety of functions. CAs are impo rtant target s for the design of novel pharmacological a gents useful in the treat ment or prevention of a variety of disorders, su ch as epilepsy and obesity. The inhibition and a ctivation of CAs are als o well unde rstood processes, with most classes of inhibitors bindin g to the metal center [۱, ۲]. In recent years the nanom aterial fulle rene C۶۰ and its derivatives have been chosen to be inve stigated for their intera ctions with CAs as an inhibitor. p resented study is an in vestigation of the comp lexes formed between a ctive site of CA enzym e and the phenylalanine derivative of fulleren e as a nanoscale inhibito r from three different positions, ۱:N۵, ۲:N۱۳ and ۳:O۱۲, Figure ۱: B, by using of quantum mechanical calculations.

کلیدواژه ها:

Carbo nic Anhydr ase ، Fuller ene ، Inhibit or ، Complex ation energy ، QM calcula tion.