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The Two‐Step Assemblies of Basic‐Amino‐Acid‐Rich Peptide with a Highly Charged Polyoxometalate
Author(s) -
Zhang Teng,
Li HongWei,
Wu Yuqing,
Wang Yizhan,
Wu Lixin
Publication year - 2015
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201501243
Subject(s) - polyoxometalate , isothermal titration calorimetry , peptide , chemistry , europium , combinatorial chemistry , amino acid , peptide sequence , biophysics , crystallography , biochemistry , organic chemistry , ion , biology , gene , catalysis
Two‐step assembly of a peptide from HPV16 L1 with a highly charged europium‐substituted polyoxometalate (POM) cluster, accompanying a great luminescence enhancement of the inorganic polyanions, is reported. The mechanism is discussed in detail by analyzing the thermodynamic parameters from isothermal titration calorimetry (ITC), time‐resolved fluorescent and NMR spectra. By comparing the actions of the peptide analogues, a binding process and model are proposed accordingly. The driving forces in each binding step are clarified, and the initial POM aggregation, basic‐sequence and hydrophobic C termini of peptide are revealed to contribute essentially to the two‐step assembly. The present study demonstrates both a meaningful preparation for bioinorganic materials and a strategy using POMs to modulate the assembly of peptides and even proteins, which could be extended to other proteins and/or viruses by using peptides and POMs with similar properties.