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. 2020 Nov 10;2(12):5866–5873. doi: 10.1039/d0na00870b

Fig. 5. Contribution of hydrogen bonding to carbon dot modulation of hIAPP fibrillation. (A) ThT fluorescence curves recorded in Tris buffer (solid curves) and PB buffer (broken curves). hIAPP alone (black curves); hIAPP + Tyr-C-dots (concentration of 0.03 mg mL−1; blue curves); hIAPP + Phe-C-dots (concentration of 0.03 mg mL−1; red curves). (B) CD spectra of hIAPP alone (black spectra) and together with Tyr-C-dots (concentration of 0.05 mg mL−1; blue spectra) recorded in Tris buffer or PB buffer. Each spectrum was acquired after 24 hour incubation of the peptide or peptide/C-dot mixture.

Fig. 5