Date of Award




Document Type


Degree Name

Doctor of Philosophy (PhD)


Department of Chemistry

Content Description

1 online resource (xiii, 112 pages) : color illustrations.

Dissertation/Thesis Chair

Igor K Lednev

Committee Members

Alexander Shekhtman, Wilfredo Colón, Maksim Royzen, Mehmet Yigit


Raman spectroscopy, Amyloid, Protein folding, Ultrastructure (Biology)

Subject Categories

Analytical Chemistry


Amyloid aggregation is a specific form of protein misfolding and self-assembly related to several degenerative pathologies like Alzheimer's and Parkinson's diseases, type-II diabetes, etc. This association with deadly diseases has made amyloid fibrils the focus of intensive research for many decades. Most recently, a significant interest to protein fibrils was also due to the application of the remarkable self-assembling capabilities to form well-structured nano-biomaterials. Self-assembly of short peptide sequences into well-organized structures is another important strategy for bottom-up fabrications of nano-biomaterials. One of the most commonly used building blocks is diphenylalanine, a short dipeptide that has been identified as playing a key role in the core-recognition motif of the Alzheimer’s disease, the β-amyloid protein. X-ray crystallography and solution NMR, two major tools of structural biology, have significant limitations when applied to such structures because of their non-crystalline and insoluble nature as well as large molecular weight.