pH-Dependent Reversible Self-Assembly of ß-Lactoglobulin-Derived Reducing Peptides.

ABSTRACT

Peptide-based self-assembled nanostructures are emerging vehicles for nutrient delivery and interface engineering. The present study screened eight ß-lactoglobulin (ß-Lg) derived peptides and found that two reducing peptides [EQSLVCQCLV (EV-10) and VCQCLVR (VR-7)] demonstrated pH-dependent reversible fibrilization. EV-10 formed fibrils at pH 2.0 but became unordered aggregates at pH 7.0. VR-7 showed the opposite trend. Both peptides could undergo repetitive transitions between fibrils and unordered aggregates during consecutive pH-cycling. Fibrilization of both peptides was dominated by charges carried by N- and C-terminals. Both fibrils were characterized by a cross-ß sheet structure where the ß-sheet was arranged in an antiparallel manner. Fe3+ was reduced by Cys and EV-10 (pH 5.0 and 7.0) simultaneously upon mixing. In contrast, EV-10 fibrils released Fe3+ reducing capacity progressively, which were beneficial to long-term protection Fe2+. The EV-10 fibrils remained intact after simulated gastric digestion and finally dissociated after intestinal digestion. The results shed light on the mechanisms of fibrilization of ß-Lg derived peptides. This study was beneficial to the rational design of smart pH-responsive materials for drug delivery and antioxidants for nutrients susceptible to oxidation.