PMC:7594251 / 81588-82754 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7594251","sourcedb":"PMC","sourceid":"7594251","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7594251","text":"Another example of practical application of ssNMR is the work of Lee and colleagues [363] in which they investigated the structure of a designed zinc-binding amyloid fibril that catalyzed ester hydrolysis. Metals ions such as zinc where found to affect the process of protein aggregation which resulted in arise of amyloid like structures. Therefore, understanding the processes of aggregation and the factors related to them is crucial for creation of new drugs for amyloid related diseases [364]. In the experiment Lee et al. used Ac-IHVHLQI-CONH2 peptide (referred as HHQ) to form fibrils with varying Zn2+:HHQ molar ratios. The results showed that Zn2+-bound HHQ fibrils form parallel-in-register form of packing β-strand in each sheet and His residues are coordinated to Zn2+ via Nδ1, while half of the His residues are also coordinated to Zn2+ via Nε2. Additionally, Zn2+ binds in a 1:1 metal ion/peptide ratio. After further analysis using structural bioinformatics, it was concluded that each zinc ion was coordinated by three histidine nitrogens from two adjacent strands. Half of all histidines bridged to Zn2+ ions forming a metal–imidazolate chain 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