Membrane-binding peptides have significant potential applications, such as antimicrobials, biosensors and in the purification of extracellular vesicles. However, to ensure the effective implementation of these peptides in biotechnological applications, it is essential to prioritize their selectivity. The Opi1 peptide has previously been shown to exhibit a high affinity for phosphatidic acid (PA)-containing membranes. Given the analogous structure of cardiolipin (CL), this proposal posits that it may be possible to develop an Opi1 variant that interacts selectively with CL-containing membranes with diverse CL proportions. Cardiolipin (CL) is exclusively found in the inner membrane of mitochondria and bacteria, making this phospholipid an interesting candidate for the design of selective peptides. The project will entail the implementation of in silico mutations of the Opi1 sequence, in order to identify novel sequences with different affinity to model membranes. The optimization and analysis of peptide-membrane interactions will be conducted through the use of atomic-resolution molecular simulations, alchemical transformations, and experimental biophysical techniques, such as liposome flotation methods and quartz crystal microbalance assay. This interdisciplinary project integrates biology, physics, and chemistry, leveraging advanced computational and experimental techniques to achieve the objectives. The interdisciplinary integration ensures robust outcomes, with potential applications in targeted drug delivery, and diagnostics, ultimately advancing our understanding of peptide-membrane interactions.

Cíle udržitelného rozvoje

Masarykova univerzita se hlásí k cílům udržitelného rozvoje OSN, jejichž záměrem je do roku 2030 zlepšit podmínky a kvalitu života na naší planetě.