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Mesoporous silica composites filling densely peptide assemblies (Proteosilica) were newly synthesized as transparent films. Spiropyran guest was co-doped in the films and photo-isomerization between spiropyran form and merocyanine form was repeated by alternate irradiation of visible and UV lights. Circular dichroism (CD) active spectra were observed only for the spiropyran form in the Proteosilica with hexagonal geometry. However, the CD active behavior was absent for the spiropyran in lamellar Proteosilica. Difference in peptide assembling structures would affect chiral sensitivity of the doped spiropyran guest.

This paper proposes a new paradigm for the biophysical concept of measuring the affinity of molecular complexes, based on a matrix representation of biological interactions and subsequent numerical analysis of the stability of this matrix. Our numerical criterion of stability (lg(cond($W$))) correlates well with experimental values such as $K_d$ and IC${}_{50}$ as well as with experimental data of aggregation kinetics in studies of amyloid peptides. The main goal of this work is to reduce the cost of biochemical experiments by obtaining preliminary information on the interaction of chemical compounds. The paper also presents our numerical calculations in comparison with a large amount of experimental data on the examples of binding of small chemical molecules gefitinib, erlotinib, imatinib, naquatinib, and CO-1686 with proteins, protein–peptide interactions of the Bcl-2 protein family, antibody–antigen CD20–rituximab, and aggregation of amyloid peptides. The description of the software package that implements the presented algorithm is given on the website: https://binomlabs.com/.

With the demonstration of direct electron transfer between the redox active prosthetic group, flavin adenine dinucleotide (FAD), of glucose oxidase (GOx) and single-walled carbon nanotubes (SWCNT), there has been growing interest in the fabrication of CNT-enzyme supramolecular constructs that control the placement of SWCNTs within the tunneling distance of co-factors for enhanced electron transfer efficiency in generation-3 biosensors and advanced biofuel cells. These conjugate systems raise a series of questions such as: which peptide sequences within the enzymes have high affinity for the SWCNTs? And, are these high affinity sequences likely to be in the vicinity of the redox-active co-factor to allow for direct electron transfer? Phage display has recently been used to identify specific peptide sequences that have high affinity for SWCNTs. Molecular dynamics simulations were performed to study the interactions of five discrete peptides with (16,0) SWCNT in explicit water as well as with graphene. From the progression of the radius of gyration, R_g, the peptides studied were concertedly adsorbed to both the SWCNT and graphene. Peptide properties calculated using individual amino acid values, such as hydrophobicity indices, did not correlate with the observed adsorption behavior as quantified by R_g, indicating that the adsorption behavior of the peptide was not based on the individual amino acid residues. However, the R_g values, reflective of the physicochemical embrace of the surface (SWCNT or graphene) had a strong positive correlation with the solubility parameter, indicating concerted, cooperative interaction of peptide segments with the materials. The end residues appear to dominate the progression of adsorption regardless of character. Sequences identified by phage display share some homology with key enzymes (GOx, lactate oxidase and laccase) used in biosensors and enzyme-based biofuel cells. These analogous sequences appear to be buried deep within the shell of fully folded proteins and as such are expected to be close to the redox-active prosthetic group.

The present article reviews the self-assembly of oligopeptides to form nanostructures, both in solution and in solid state. The solution structures of the peptides were examined using circular dichroism and dynamic light scattering. The solid state assembly was examined by adsorbing the peptides onto a mica surface and analyzing it using atomic force microscopy. The role of pH and salt concentration on the peptide self-assembly was also examined. Nanostructures within a size range of 3–10 nm were obtained under different conditions.