Experimental characterization and simulation of amino acid and peptide interactions with inorganic materials

Abstract

Inspired by nature, many applications and new materials benefit from the interplay of inorganic materials and biomolecules. A fundamental understanding of complex organic–inorganic interactions would improve the controlled production of nanomaterials and biosensors to the development of biocompatible implants for the human body. Although widely exploited in applications, the interaction of amino acids and peptides with most inorganic surfaces is not fully understood. To date, precisely characterizing complex surfaces of inorganic materials and analyzing surface–biomolecule interactions remain challenging both experimentally and computationally. This article reviews several approaches to characterizing biomolecule–surface interactions and illustrates the advantages and disadvantages of the methods presented. First, we explain how the adsorption mechanism of amino acids/peptides to inorganic surfaces can be determined and how thermodynamic and kinetic process constants can be obtained. Second, we demonstrate how this data can be used to develop models for peptide–surface interactions. The understanding and simulation of such interactions constitute a basis for developing molecules with high affinity binding domains in proteins for bioprocess engineering and future biomedical technologies.

Bare Iron Oxide Nanoparticles for Magnetic Harvesting of Microalgae: From Interaction Behavior to Process Realization

“…Accordingly, they have been the subject of numerous studies on their interaction with various biomolecules [ 17 , 18 , 19 ] and with whole cell systems [ 20 , 21 ]. Among others, we are investigating the interactions of magnetic nanoparticles with amino acids [ 22 ], peptides [ 23 , 24 ], and proteins [ 25 , 26 , 27 ], as well as their technical application in high-gradient magnetic separation, for meeting downstream processing goals [ 28 , 29 ]. The main advantages of magnetic separation processes are the high efficiency and the low operating costs, together with simple and fast processing.…”

Molecular Modeling and Simulation Tools in the Development of Peptide-Based Biosensors for Mycotoxin Detection: Example of Ochratoxin

“…The overall performance of a biosensor system is directly influenced by the mycotoxin-binding properties of the molecular recognition bioreceptor. The design and fabrication of the biotransducer involves the immobilization of the peptides receptor on the insoluble phases of physicochemical transducers such as metallic electrodes, composites, ceramics, and polymers in a plurality of formats such as polymer foams, polymer membranes, hydrogels, nanomaterials, and films [ 54 , 55 , 56 ]. A generic approach to peptide immobilization involve support choices that are relatively cheap and easy to obtain, but provides a high surface-to-volume ratio to facilitate a dense packing of the peptides.…”

“…The goal of which was to better predict the strength of non-specific interaction between the peptide receptors containing different primary sequence and diverse exposed functional groups on the material’s surface. However, different homopeptide studies and experimental binding studies on tandem repeat peptide sequences have demonstrated that the interfacial binding strength of a given sequence is not an additive sum of the binding strengths of the individual residues [ 91 ], but is instead influenced by the structure and order of the peptide sequences [ 55 , 78 ]. The strength of H-bond interactions between the material-solvent further determines the extent of desolvation of the peptide.…”

Buffer Influence on the Amino Acid Silica Interaction

“…There have been a number of studies that investigated such interactions for metal, metal oxide, polymer or silica surfaces both experimentally and theoretically, [5][6][7] but trends for peptides have been difficult to derive due to complexities of the composition of the system. [8] The latter comprises not only the peptide and the surface but also the solvent, which often contains a buffer to stabilize the pH of the system. The fact that buffer ions can compete with the peptide/ protein in binding to the surface is well known and investigated, [9][10][11][12][13][14][15][16][17][18][19][20] but to the best of our knowledge this has never been done for single amino acids especially for silica.…”

“…However, it is difficult to characterize these interactions for small peptides or individual amino acids (AAs). There have been a number of studies that investigated such interactions for metal, metal oxide, polymer or silica surfaces both experimentally and theoretically, but trends for peptides have been difficult to derive due to complexities of the composition of the system . The latter comprises not only the peptide and the surface but also the solvent, which often contains a buffer to stabilize the pH of the system.…”