Journal
LANGMUIR
Volume 38, Issue 22, Pages 7077-7084Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.langmuir.2c00904
Keywords
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Funding
- National Research Foundation of Korea (NRF) - Ministry of Science, ICT & Future Planning (M S I P) [019R1C1C1009111, 2020R1C1C1008886]
- GRRC program of Gyeonggi province [GRRC-kyunghee2017(A01)]
- National Research Foundation of Korea [2020R1C1C1008886] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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This manuscript demonstrates that short peptides self-associated into amyloid fibers with metal ion-binding ability can exhibit melanosomal functions. The coordinated metal ions and the amyloid structure itself have different functions in accelerating oxidative self-association of dopamine and regulating material properties.
Short peptides designed to self-associate into amyloidfibers with metal ion-binding ability have been used to catalyzevarious types of chemical reactions. This manuscript demonstrates that one of these short-peptidefibers coordinated with CuIIcanexhibit melanosomal functions. The coordinated CuIIand the amyloid structure itself are differentially functional in acceleratingoxidative self-association of dopamine into melanin-like species and in regulating their material properties (e.g., water dispersion,morphology, and the density of unpaired electrons). The results have implications for the role of functional amyloids in melaninbiosynthesis and for designing peptide-based supramolecular structures with various emergent functions.
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