Tryptophan-Laurdan interaction in ester and ether PC membrane interfaces

PÉREZ HUGO; GONZÁLEZ PAZ AGUSTÍN NICOLÁS; DISALVO ANIBAL; FRÍAS MARÍA DE LOS ÁNGELES

San Luis

Congreso; XLVIII Reunión Anual de la Sociedad Argentina de Biofísica; 2019

Universidad Nacional de San Luis

Numerous investigations have been carried out to interpret the role of tryptophan (Trp) in the peptides and proteins (such as melittin, annexins, among other molecules of biological importance) interaction with lipid membranes through various techniques, such as NMR, FTIR, X ray diffraction, among others. In particular, studies using Laurdan as a fluorescent probe has been extensively done to have an insight on the hydration states of the interface. In this regard, the presence or absence of hydration centers such as carbonyl groups can be decisive in the interaction of Trp with membranes. In this work, the interaction of Trp with lipid membranes models composed of ester and ether lipids of different chain lengths in the presence of the Laurdan fluorescent probe is studied.