Spectroscopic investigation on gel‐forming β‐sheet assemblage of peptide derivatives

The conformational studies of peptide derivatives A and B in a gel state were studied by using circular dichroism (CD), Fourier transformed infrared (FTIR), and fluorescence spectroscopic techniques. Birefringence and electron microscopic studies were carried out to characterize the morphological aspects of the fibrils in the gel. The FTIR spectra of the peptides show the absence of free NH in the gel state, implying that the intermolecular hydrogen‐bond formation is the driving force for the aggregation. The CD spectrum of the peptide gels shows the presence of antiparallel and parallel β‐sheet conformation for peptide derivatives A and B , respectively. Electron microscopic studies (EM) of the peptide derivatives A and B reveal that peptide A formed rigid, rod‐like structures without cross‐linking and peptide B formed loose fibrils organized into highly noncovalently cross‐linked mesh‐like structural aggregates. Peptide A was much more soluble in alcoholic solvents than peptide B , and no birefringence was observed with Congo red (CR) staining in the temperature range of 0–80°C. The spectroscopic studies indicate that peptide B consists of domains having a significant amount of β‐sheet structure and exhibiting golden yellow birefringence between 53 and 56°C when stained with Congo red. On the other hand, peptide A gives no evidence of birefringence under polarized light. Fluorescence probe binding studies with pyrene in gel state with peptides A and B indicates the polarity in the interior of the aggregates. The data presented in the present work indicate that peptide B forms fibrils, which is similar to amyloid aggregates that are present in biological systems. © 2003 Wiley Periodicals, Inc. Biopolymers 70: 346–354, 2003