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• W2503670048 abstract "Pif is a crucial protein for the formation of the nacreous layer in Pinctada fucata. Three non-acidic peptide fragments of the aragonite-binding domain (Pif80) are selected, which contain multiple copies of the repeat sequence DDRK, to study the interaction between non-acidic peptides and aragonite. The polypeptides DDRKDDRKGGK (Pif80-11) and DDRKDDRKGGKDDRKDDRKGGK (Pif80-22) have similar binding affinity to aragonite. Solid-state NMR data indicate that the backbones of Pif80-11 and Pif80-22 peptides bound on aragonite adopt a random-coil conformation. Pif80-11 is a lot more effective than Pif80-22 in promoting the nucleation of aragonite on the substrate of β-chitin. Our results suggest that the structural arrangement at a protein-mineral interface depends on the surface structure of the mineral substrate and the protein sequence. The side chains of the basic residues, which function as anchors to the aragonite surface, have uniform structures. The role of basic residues as anchors in protein-mineral interaction may play an important role in biomineralization." @default.
• W2503670048 created "2016-08-23" @default.
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• W2503670048 date "2016-08-01" @default.
• W2503670048 modified "2023-10-16" @default.
• W2503670048 title "Study of Binding Interaction between Pif80 Protein Fragment and Aragonite" @default.
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• W2503670048 doi "https://doi.org/10.1038/srep30883" @default.
• W2503670048 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4971512" @default.
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