Obtaining site-specific structural information would also be useful in developing our technique. Residue-specific structural information could conceivably be obtained through sitespecific labeling schemes of amide nitrogen and carbon atoms. Since the pathophysiologically-relevant lengths of many amyloidogenic proteins, including amylin, are generally less than 50 amino acids, isotopic editing of peptides could be achieved using solid-phase synthesis. Isotopic labeling of the peptide backbone carbon and nitrogen atoms would decouple the NH bending, CN stretching, and C--O stretching motions in amide vibrations. Isolating the corresponding Amide I and III modes for individual residues could therefore be achieved by determining the difference spectra between the isotopically labeled and unlabeled fibril species. Thus, with these current limitations, it is clear that follow-up studies are needed to increase the utility of our methodology. Despite this, however, we believe that our approach lays a foundation towards potentially using Raman spectroscopy with MD to visualize the three-dimensional structures of amyloid fibrils and other biological macromolecules. Spectroscopy Society of Pittsburgh (DP and MH), and the National Institutes of Health (P20 GM1350007) through the Vermont Center for Cardiovascular and Brain Health pilot grant award (DP, YO, MH, and UN). The Raman microscope used in this work was purchased from funds provided by the National Science Foundation (DMR-1919610). The AFM used in this work was purchased from funds provided by the National Center for Research Resources (S10RR025498).