Abstract

Nanoscale surface topographies mediated with biochemical cues influence the differentiation of stem cells into different lineages. This research focuses on the adsorption behavior of bone morphogenetic protein (BMP-2) on nanopatterned gold substrates, which can aid in the differentiation of bone and cartilage tissue constructs. The gold substrates were patterned as flat, pillar, linear grating, and linear-grating deep based, and the BMP-2 conformation in end-on configuration was studied over 20 ns. The linear grating deep substrate pattern had the highest adsorption energy of around 125 kJ/mol and maintained its radius of gyration of 18.5 Å, indicating a stable adsorption behavior. Secondary structures including α-helix and β-sheet displayed no denaturation, and thus, the bioavailability of the BMP-2, for the deep linear-grating pattern. Ramachandran plots for the wrist and knuckle epitopes indicated no steric hindrances and provided binding sites to type I and type II receptors. The deep linear-grating substrate had the highest number of contacts (88 atoms) within 5 Å of the gold substrate, indicating its preferred nanoscale pattern choice among the substrates considered. This research provides new insights into the atomistic adsorption of BMP-2 on nanoscale topographies of a gold substrate, with applications in biomedical implants and regenerative medicine.

Highlights

  • Protein adsorption on a biomaterial for tissue engineering applications relies on the conformational and orientation behavior of the protein to obtain biological responses, including biocompatibility and cellular interactions [1,2]

  • The end-on configurations had favorable adsorption characteristics, along with a robust secondary structure. These four orientations were further studied with hydrophobic and hydrophilic flat substrates [31]

  • The protein was placed in an end-on orientation on the top center of four gold substrates: flat (FLT), pillars (FLT), shallow linear grating (SLG), and deep linear grating (DLG)

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Summary

Introduction

Protein adsorption on a biomaterial for tissue engineering applications relies on the conformational and orientation behavior of the protein to obtain biological responses, including biocompatibility and cellular interactions [1,2]. The end-on configurations had favorable adsorption characteristics, along with a robust secondary structure These four orientations were further studied with hydrophobic (gold) and hydrophilic (silicon nitride) flat substrates [31]. The protein was placed in an end-on orientation on the top center of four gold substrates: flat (FLT), pillars (FLT), shallow linear grating (SLG), and deep linear grating (DLG) This specific orientation improves BMP-2 adsorption on silicon dioxide, silicon nitride, and gold [30,31,32]. A previous study indicated that in flat gold, a hydrophobic substrate, the solvent can restrict the protein movement, preventing residues from adsorbing [32] This occurred because the wetting of the gold surface directly influences the protein behavior, building a barrier that inhibits adsorption. Higher conformationAalftcehra2n0gness occurred in the patterned souccrfuaSrctreresud,cctfouomrreaplal rceoSdntwfirugictuthuraflrteaiot npsa,ttwerhnFislca.htNreolasitgesnitfioctahPneitlladabirsilriutyptoiof nthGLoerfianhttheyiaendrgsroecpohnoLdbiaiinnrcyegsaosDrtlrvGeueercnpattut-troe limit tαh-eheplrioxtein mo10v.e3m8%ent on go1l0d.3s8u%rfaces [31]1. 5D.0L9G%lost part1o1.f3i2ts%α-helix a9n.d43β%-sheet struc3tu10r-ehse,ltixhus tran0s.f0o0r%ming into0a.0c0o%il structure.2.83%

Linear Grating Deep
Conclusions
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