Arginine Residues Modulate the Membrane Interactions of pHLIP Peptides.

ABSTRACT: Most processes at the water-membrane interface often involve protonation events in proteins or peptides that trigger important biological functions and events. This is the working principle behind the pHLIP peptide technology. A key titrating aspartate (Asp14 in wt) is required to protonate to induce the insertion process, increase its thermodynamic stability when membrane-embedded, and trigger the peptide's overall clinical functionality. At the core of pHLIP properties, the aspartate pK_a and protonation are a consequence of the residue side chain sensing the changing surrounding environment. In this work, we characterized how the microenvironment of the key aspartate residue (Asp13 in the investigated pHLIP variants) can be modulated by a simple point mutation of

SUBMITTER: Silva TFD 

PROVIDER: S-EPMC10369490 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature