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Design of Amphiphilic Peptide Geometry towards Biomimetic Self‐Assembly of Chiral Mesoporous Silica
Author(s) -
Huang Zhehao,
Yao Yuan,
Che Shunai
Publication year - 2014
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.201304400
Subject(s) - amphiphile , mesophase , chirality (physics) , peptide , lamellar structure , self assembly , hydrogen bond , mesoporous silica , materials science , intermolecular force , supramolecular chirality , supramolecular chemistry , molecule , crystallography , chemistry , combinatorial chemistry , chemical engineering , mesoporous material , nanotechnology , organic chemistry , copolymer , catalysis , polymer , phase (matter) , chiral symmetry breaking , quark , biochemistry , quantum mechanics , nambu–jona lasinio model , physics , engineering
In nature, diatoms and sponges are exquisite examples of well‐defined structures produced by silica biomineralisation, in which proteins play an important role. However, the artificial peptide templating route for the silica mesostructure remains a formidable and unsolved challenge. Herein, we report our effort on the design of amphiphilic peptides for synthesising a highly ordered two‐dimensional (2D)‐hexagonal and lamellar chiral silica mesostructure using trimethoxysilylpropyl‐ N , N , N ‐trimethylammonium chloride as the co‐structure directing agent (CSDA). The geometry of the peptide was designed by adding proline residues into the hydrophobic chain of the peptide to break the β‐sheet conformation by weakening the intermolecular hydrogen bonds; this led to the mesophase transformation from the most general lamellar structure to the 2D hexagonal P 6 mm mesostructure by increasing the amphiphilic molecules packing parameter g . Enantiomerically pure chiral mesostructures were formed thanks to the intrinsic chirality and relatively strong intermolecular hydrogen bonds of peptides.