The affinity of biomolecules,
such as peptides and proteins, with
inorganic surfaces, is a fundamental topic in biotechnology and bionanotechnology.
Amino acids are often used as “model” bits of peptides
or proteins for studying their properties in different environments
and/or developing functional surfaces. Despite great demand for knowledge
about amino acid interactions with metal oxide surfaces, studies on
the issue represent a fragmentary picture. In this paper, we describe
amino acid adsorption on nanocrystalline anatase systematically at
uniform conditions. Analysis of the Gibbs free adsorption energy indicated
how the aliphatic, aromatic, polar, and charged side chain groups
affect the binding affinity of the amino acids. Thermodynamic features
of the l-amino acid adsorption receive thorough interpretation
with calculated molecular descriptors. Theoretical modeling shows
that amino acids complex with TiO2 nanoparticles as zwitterions
via ammonium group.
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