Impact of peptide conformation and flexibility on the adsorption behavior on silica surfaces. Panel (A): scheme of the suggested interaction of peptide LK14 (Ac-LKKLLKLKLLKLK-NH2) with a negatively charged silica surface. The peptide maintains an amphiphilic α-helix structure with charged lysine and hydrophobic leucine residues on opposite sides. Reprinted with permission from [138]. Copyright (2009) American Chemical Society. Panel (B): (Top) Ramachandran plots for peptides S1 (PPPWLPYMPPWS), S2 (LPDWWPPPQLYH), and W1 (EVRKEVVAVARN) in solution generated from MD trajectories. Peptide W1 explore more φ and ψ angles compared to S1 and S2, which indicates more configurational sampling. (Bottom) Snapshots of peptides interacting with a quartz (100) surface from the strongest binding MD trajectories. Peptides S1 and S2 exhibit stronger surface interactions compared to W1 (key interacting residues are highlighted). Reprinted with permission from [26]. Copyright (2010) American Chemical Society. Panel (C): (Left) adsorption of peptides pep1 (KSLSRHDHIHHH) and its mutant variants pep1_6 (KSLSRADHIHHH) and pep1_11 (KSLSRHDHIHAH). The adsorption order is pep1_6 > pep1 > pep1_11 for initial peptide concentrations up to 2 mg ml⁻¹ (pH 7.5, 100 mM phosphate, 150 mM NaCl). (Right) Scheme of peptide interactions with a negatively charged silica surface, showing the impact of His-6 and His-11 mutations on backbone flexibility and binding strength. Reprinted with permission from [24]. Copyright (2012) American Chemical Society.