Modeling‐Led Materials‐Binding Peptide Design for Hexagonal Boron Nitride Interfaces

Abstract

For example, the P1 peptide, [17,18] with sequence HSSWYWAFNNKT, is one of the most studied graphene recognizing biomolecules due to its binding affinity on basal graphene. It has been previously demonstrated that using a sonication-based exfoliation method and the P1 peptide, one can obtain exfoliated graphene with a thickness of <2 nm that remains colloidally dispersed in aqueous systems. [11,17,18] Fatty-acid modification on either the N-or C-terminal of P1 also binds graphene strongly and brings similar exfoliation outcomes along with significant reduction of sheet damage, proposed to be conferred via edge-wrapping mechanisms. [11,19] However, the use of peptide-based approaches is not limited to exfoliation and dispersion, since peptides can also be adapted to organize and activate these 2D materials for integration into, for example, sensors, photonics, and biomedical devices. For example, peptide-based superstructures with welldefined self-assembled peptide nanofibers adsorbed onto graphene oxide (GO) have shown high stability/sensitivity for electrochemical sensing of H 2 O 2 . [20][21][22] Likewise, hexagonal boron nitride (h-BN) is also a promising 2D nanomaterial. Structurally similar to graphene, the boron and nitrogen atoms are arranged in a hexagonal lattice in a single layer. h-BN nanosheets have many unique properties, for instance, the wide bandgap of 5.5-5.9 eV and high thermal stability which makes it an ideal insulator, [23,24] and can provide an excellent biomedical imaging platform with good biocompatibility. [25][26][27] To obtain h-BN sheets, the exfoliation approach is intriguing, [28][29][30][31] and there is scope for identifying similar biomolecule-mediated strategies via the exploitation of highly specific noncovalent interactions. However, there is very limited knowledge regarding how biomolecules interact with the h-BN surface. BP1 (LLADTTHHRPWT) and BP7 (VDAQSKSYTLHD) are currently two peptide sequences identified with binding affinity with h-BN nanospheres and nanosheets. [32] Fattyacid attachment onto the BP7 peptide was shown to increase the binding strength with the h-BN surface, [33,34] but a deeper understanding is required to design and manipulate the interface between peptides and the h-BN surface.This task is challenging to accomplish by experimental efforts alone, and molecular dynamics (MD) simulations can provide complementary insights to provide a fundamental basis for materials-binding peptide design. However, the lack of a Peptides that can bind specific nanomaterials with affinity and specificity are attractive for realizing a wide range of applications. Manipulation of biomolecule/2D-material interfaces via noncovalent interactions in aqueous media has gained intensive attention due to the promising potential for biomolecule-facilitated 2D-material exfoliation, dispersion, and organization in water. Such advances have been recently achieved for graphene, where several peptide sequences have demonstrated this capability. However, few peptides are known specific bind...

Single Amino Acid Modifications for Controlling the Helicity of Peptide-Based Chiral Gold Nanoparticle Superstructures

“…The umbrella sampling approach was used to evaluate the potential of mean force profiles for the amino acid analogues of the M ox , CtBu, and C ox tBu residues, binding at the aqueous Au(111) interface. The amino acid binding energy profiles were calculated using a methodology similar to that published previously . Both the N- and C-termini of the amino acids were capped.…”

“…The amino acid binding energy profiles were calculated using a methodology similar to that published previously. 30 Both the N-and C-termini of the amino acids were capped. Steered pulling simulations were conducted to obtain configurations as a function of vertical distance from the surface in the z-direction.…”