Study of binding interaction between Pif80 protein fragment and aragonite

Please use this identifier to cite or link to this item: https://ir.lib.ncu.edu.tw/handle/987654321/101844

Title:	Study of binding interaction between Pif80 protein fragment and aragonite
Authors:	杜遠朋;Du, Yuan-Peng;Chang, Hsun-Hui;Yang, Sheng-Yu;Huang, Shing-Jong;Tsai, Yu-Ju;Huang, Joseph Jen-Tse;Chan, Jerry Chun Chung
Contributors:	理學院化學學系
Keywords:	639/301/54/1754;639/301/930/878/1264;Amino acid sequence;Animals;Calcium Carbonate - chemistry;Calcium Carbonate - metabolism;Chitin;Crystallization;Extracellular Matrix Proteins - chemistry;Extracellular Matrix Proteins - metabolism;Humanities and Social Sciences;Mineralization;multidisciplinary;Nucleation;Peptide Fragments - chemistry;Peptide Fragments - metabolism;Peptides;Pinctada - metabolism;Protein Binding;Proteins;Science;Science (multidisciplinary)
Date:	2016-08-03
Issue Date:	2026-04-21 14:47:50 (UTC+8)
Publisher:	Nature Publishing Group;London: Nature Publishing Group UK
Abstract:	摘要： 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. 其他題名： Sci Rep 出版者： London: Nature Publishing Group UK 出版日期： 2016-08-03 出處： Scientific reports, 2016-08, Vol.6 (1), p.30883-30883, Article 30883 資源來源： Publicly Available Content Database 版權： The Author(s) 2016 版權： Copyright Nature Publishing Group Aug 2016 版權： Copyright © 2016, The Author(s) 2016 The Author(s) 識別號： ISSN: 2045-2322 識別號： EISSN: 2045-2322 識別號： DOI: 10.1038/srep30883 識別號： PMID: 27484975
Appears in Collections:	[Department of Chemistry] journal & Dissertation

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