Length and Charge of Water-Soluble Peptoids Impact Binding to Phospholipid Membranes
| Autor: | Anna L. Calkins, Fabiola L Gutierrez, Grace Y. Stokes, Kalli M. Dowell, Madeleine R. Landry, Morgan A MacKenzie, Jacenda L. Rangel, Amelia A. Fuller, Vivian P Dao |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Phospholipid
010402 general chemistry 01 natural sciences chemistry.chemical_compound symbols.namesake Peptoids Adsorption 0103 physical sciences Materials Chemistry Molecule Physical and Theoretical Chemistry Lipid bilayer Phospholipids Aqueous solution Binding Sites 010304 chemical physics Molecular Structure Langmuir adsorption model Water Peptoid Hydrogen-Ion Concentration 0104 chemical sciences Surfaces Coatings and Films Membrane chemistry Solubility Biophysics symbols lipids (amino acids peptides and proteins) |
| Zdroj: | The journal of physical chemistry. B. 123(27) |
| ISSN: | 1520-5207 |
| Popis: | In this study, we provide a quantitative description of the adsorption of water-soluble N-substituted glycine oligomers (peptoids) to supported lipid bilayers that mimic mammalian plasma membranes. We prepared a small array of systematically varied peptoid sequences ranging in length from 3 to 15 residues. Using the nonlinear optical method second harmonic generation (SHG), we directly monitored adsorption of aqueous solutions of 3- and 15-residue peptoids to phospholipid membranes of varying physical phase, cholesterol content, and head group charge in physiologically relevant pH buffer conditions without the use of extrinsic labels. Equilibrium binding constants and relative surface coverages of adsorbed peptoids were determined from fits to the Langmuir model. Three- and 15-residue peptoids did not interact with cholesterol-containing lipids or charged lipids in the same manner, suggesting that a peptoid’s adsorption mechanism changes with sequence length. In a comparison of four three-residue peptoids... |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|