Complementary Surface-Enhanced Raman Scattering (SERS) and IR Absorption Spectroscopy (SEIRAS) with Nanorods-on-a-Mirror

The surface-enhanced counterparts of Raman scattering (SERS) and infrared (IR) absorption (SEIRAS) are commonly used to probe and identify nanoscale matter and small populations of molecules. The contrasting selection rules offer complementary vibrational information of bulk solids or solutions. In this study, a complementary surface-enhanced vibrational spectroscopy approach is presented to probe the vibrational signature of metal-bound molecular monolayers. Nanocavities are designed and produced with sharp and tunable visible (VIS) and mid-IR gap resonances by placing nanorods on a mirror that is coated with a thin dielectric spacer. Their VIS resonances are tuned to match a 1.61 eV (770 nm) resonant excitation for SERS, while their mid-IR resonances span the 1500–2800 cm⁻¹ range (6.5–3.5 µm) in high resolution for SEIRAS, targeting CN bond vibrations at 2220 cm⁻¹. Both the VIS and mid-IR gap modes support spatially overlapping and highly enhanced near-fields ensuring strong SERS and SEIRAS signals from the same monolayer molecular population. The differences in the vibrational information obtained with the two surface-enhanced spectroscopies when probing coupled molecular vibrations are highlighted and the advantages of using such a platform for investigating cavity-modified chemical reactions are discussed.     

Selection of peptides targeting helix 31 of bacterial 16S ribosomal RNA by screening M13 phage-display libraries

Ribosomal RNA is the catalytic portion of ribosomes, and undergoes a variety of conformational changes during translation. Structural changes in ribosomal RNA can be facilitated by the presence of modified nucleotides. Helix 31 of bacterial 16S ribosomal RNA harbors two modified nucleotides, m2G966 and m?C967, that are highly conserved among bacteria, though the degree and nature of the modifications in this region are different in eukaryotes. Contacts between helix 31 and the P-site tRNA, initiation factors, and ribosomal proteins highlight the importance of this region in translation. In this work, a heptapeptide M13 phage-display library was screened for ligands that target the wild-type, naturally modified bacterial helix 31. Several peptides, including TYLPWPA, CVRPFAL, TLWDLIP, FVRPFPL, ATPLWLK, and DIRTQRE, were found to be prevalent after several rounds of screening. Several of the peptides exhibited moderate affinity (in the high nM to low μM range) to modified helix 31 in biophysical assays, including surface plasmon resonance (SPR), and were also shown to bind 30S ribosomal subunits. These peptides also inhibited protein synthesis in cell-free translation assays.