Figure - available from: Journal of Physics: Condensed Matter
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![Peptide–peptide association and binding on silica surfaces. Top panel illustrates the interaction of the charge-neutral peptide AFILPTG with other peptides and the silica surface at pH 7; the qualitative adsorption behavior depends on peptide concentration. The scheme highlights the influence of van der Waals interactions as peptide concentration increases. The bottom graph shows adsorption isotherms comparing the binding behavior of three different peptides on SiO2 (82 nm): S1 (KLPGWSG, circles), S2 (AFILPTG, triangles), and S3 (LDHSLHS, squares). The dotted line indicates hypothetical 100% adsorption for reference. Reprinted with permission from [114]. Copyright (2012) American Chemical Society.](publication/390291282/figure/fig4/AS:11431281396151770@1745473923453/Peptide-peptide-association-and-binding-on-silica-surfaces-Top-panel-illustrates-the.jpg)
Peptide–peptide association and binding on silica surfaces. Top panel illustrates the interaction of the charge-neutral peptide AFILPTG with other peptides and the silica surface at pH 7; the qualitative adsorption behavior depends on peptide concentration. The scheme highlights the influence of van der Waals interactions as peptide concentration increases. The bottom graph shows adsorption isotherms comparing the binding behavior of three different peptides on SiO2 (82 nm): S1 (KLPGWSG, circles), S2 (AFILPTG, triangles), and S3 (LDHSLHS, squares). The dotted line indicates hypothetical 100% adsorption for reference. Reprinted with permission from [114]. Copyright (2012) American Chemical Society.
Source publication
Silica-binding peptides (SBPs) are increasingly recognized as versatile tools for various applications spanning biosensing, biocatalysis, and environmental remediation. This review explores the interaction between these peptides and silica surfaces, offering insights into how variables such as surface silanol density, peptide sequence and compositi...
