Interactions between Membranes and “Metaphilic” Polypeptide Architectures with Diverse Side-Chain Populations

At physiological conditions, most proteins or peptides can fold into relatively stable structures that present on their molecular surfaces specific chemical patterns partially smeared out by thermal fluctuations. These nanoscopically defined patterns of charge, hydrogen bonding, and/or hydrophobicity, along with their elasticity and shape stability (folded proteins have Young’s moduli of ∼1 × 108 Pa), largely determine and limit the interactions...