Peptide Solid Surface Interface
Arch has developed a group of novel synthetic peptides and peptide...
Davis EM, Li DY, Irvin RT
Biomaterials. 2011 Aug;32(23):5311-9. Epub 2011 May 7. PubMed PMID: 21550656
A synthetic peptide derived from the native protein sequence of a metal binding bacterial pilus was observed to spontaneously react with stainless steel via a previously unreported type of chemical interaction to generate an altered form of stainless steel which we term bioorganic stainless steel. Bioorganic stainless steel has a significantly increased electron work function (4.9 ± 0.05 eV compared to 4.79 ± 0.07 eV), decreased material adhesive force (19.4 ± 8.8 nN compared to 56.7 ± 10.5 nN), and is significantly harder than regular 304 stainless steel (~40% harder). A formal or semi-formal organo-metallic covalent bond is generated between a pilin receptor binding domain and stainless steel based on XPS analysis which indicates that the electronic state of the surface is altered. Further, we establish that the peptide-steel reaction demonstrates a degree of stereospecificity as the reaction of native L-peptide, D-peptide and a retro-inverso-D-peptide yields bioorganic steel products that can be differentiated via the resulting EWF (4.867 ± 0.008 eV, 4.651 ± 0.008 eV, and 4.919 ± 0.007 eV, respectively). We conclude that electron sharing between the peptide and steel surface results in the stabilization of surface electrons to generate bioorganic steel that displays altered properties relative to the initial starting material. The bioorganic steel generated from the retro-inverso-D-peptide yields a protease stable product that is harder (41% harder at a 400 μN load), and has a 50% lower corrosion rate compared with regular stainless steel (0.11 ± 0.03 mpy and 0.22 ± 0.04 mpy, respectively). Bioorganic steel is readily fabricated.