Optimization of Amino Acid Sequence of Fmoc-Dipeptides for Interaction with Lipid Membranes

• DOI: 10.1021/acs.jpcb.9b01132
• Publication Date: 2019-04-05T12:56:47Z
• Authors: Pablo G. Argudo; Rafael Contreras-...; Luis Álvarez de C...; María T. Martín-R...; Luis Camacho; Juan J. Giner-Cas...
• Keywords: Sequence (biology)

Fmoc-dipeptides appear as highly relevant building blocks in smart hydrogels and nanovehicles for biological applications. The interactions of the with cell membrane determine efficiency nanomaterials based on Fmoc-dipeptides' internalization drug delivery. Here, we aim to understand interplay between a phospholipid surface function amino acid sequence. DMPA (1,2-dimyristoyl-sn-glycero-3-phosphate) Langmuir monolayers was used model surface. A set seven derivatives broad range hydrophobicity were included. Mixed composed DMPA/Fmoc-dipeptides an equimolar ratio built characterized situ at air/water interface. Surface pressure–molecular area isotherms (π–A), Brewster angle microscopy (BAM), UV–vis reflection spectroscopy (ΔR) combined provide holistic picture Fmoc-dipeptide molecules. An increase led enhanced interaction compression mixed monolayer could displace significant fraction from monolayer. High promoted self-assembly over these two phenomena analyzed sequence Fmoc-dipeptides. toxicity effect Fmoc-FF be observed detailed molecular level. This study suggests that adjustment within defined might optimize their lipid membranes. semiquantitative guide chemical design applications is proposed herein.