Raman microscopy comparative study of L-Cysteine, L-Cysteine Methyl ester and L-Cysteine Ethyl ester with DPPC liposomes in anhydrous state

J. M. ARIAS; M. E. TUTTOLOMONDO; S. B. DIAZ; A. BEN ALTABEF

Jena

Conferencia; ICORS2014; 2014

Cysteine is a proteinogenic biomolecule with a thiol group. It is known to act as an active site in the performance of enzymes known as cysteine proteases. Thiol is susceptible to oxidation to create a disulfide bridge between two molecules by a covalent bond. This is a very important link in the structure, folding and protein function, facilitating the stability thereof. Some proteins may undergo oxidation reduction reversibly disulfide bridges as a mechanism of redox regulation of their functions, among other properties. For these reasons we study and try to understand their interaction with the lipid membrane using model systems of DPPC liposomes in anhydrous state applying Raman microscopy.