Raman spectroscopy has long been proved to be a useful tool to study the conformation of protein‐based materials such as silk. Thanks to recent developments, linearly polarized Raman spectromicroscopy has appeared very efficient to characterize the molecular structure of native single silk fibers and spinning dopes because it can provide information relative to the protein secondary structure, molecular orientation, and amino acid composition. This review will describe recent advances in the study of the structure of silk by Raman spectromicroscopy. A particular emphasis is put on the spider dragline and silkworm cocoon threads, other fibers spun by orb‐weaving spiders, the spinning dope contained in their silk glands and the effect of mechanical deformation. Taken together, the results of the literature show that Raman spectromicroscopy is particularly efficient to investigate all aspects of silk structure and production. The data provided can lead to a better understanding of the structure of the silk dope, transformations occurring during the spinning process, and structure and mechanical properties of native fibers. © 2011 Wiley Periodicals, Inc. Biopolymers 97: 322–336, 2012.

In this study, we demonstrate the use of eco-friendly native spider silk as an efficient optical fiber in air, highly bent fibers, and physiological liquid. We also integrated the silk filament in a photonic chip made of polymer microstructures fabricated by UV lithography. The molding process is non-destructive for silk and leads to an efficient micro-optical coupling between silk and synthetic optical structures. These optical performances combined with the unique biocompatibility, bioresorbability, flexibility, and tensile strength of silk filaments pave the way for new applications in biological media and for original biophotonic purposes.

The major ampullate (MA) silk of spider is known to be composed of oriented β-sheet nanocrystals dispersed within an amorphous matrix. The presence of an interphase has also been proposed, but it has not been reported for the fibroin of the silkworm Bombyx mori (B. mori). To obtain quantitative information regarding this third phase, the deuteration of B. mori silk and Nephila clavipes MA silk has been probed by attenuated total reflection infrared spectroscopy. The spectral decomposition of the amide II region has allowed determination of the level of orientation and content of the different secondary structures. The data reveal that, in addition to the amorphous domains, part of the β-sheets is deuterated upon immersion in D₂O for both silks. The D₂O-inaccessible β-sheets are associated with crystallites, while the interphase is composed of D₂O-accessible ones. It is found that the former β-sheets are slightly more oriented along the fiber axis than the latter ones, which suggests that the interphase β-sheets are located at both ends of the crystals. The total β-sheet content is similar for B. mori silk (50 ± 4%) and MA silk (46 ± 4%). However, 27 ± 3% of the β-sheets of MA silk are D₂O-accessible compared to 8 ± 3% for B. mori silk. These data suggest that around 5 amino acids for B. mori silk and 9 amino acids for MA silk would be involved in the interphase β-sheets. The higher amount of interphase β-sheets for MA silk is believed to contribute to its higher toughness.

A microfluidic bioreactor with an easy to fabricate nano-plasmonic surface is demonstrated for studies of biofilms and their precursor materials via Surface Enhanced Raman Spectroscopy (SERS). The system uses a novel design to induce sheath flow confinement of a sodium citrate biofilm precursor stream against the SERS imaging surface to measure spatial variations in the concentration profile. The unoptimised SERS enhancement was approximately 2.5 × 10⁴, thereby improving data acquisition time, reducing laser power requirements and enabling a citrate detection limit of 0.1 mM, which was well below the concentrations used in biofilm nutrient solutions. The flow confinement was observed by both optical microscopy and SERS imaging with good complementarity. We demonstrate the new bioreactor by growing flow-templated biofilms on the microchannel wall. This work opens the way for in situ spectral imaging of biofilms and their biochemical environment under dynamic flow conditions.