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The Structural and Thermodynamic Basis for the Formation of Self‐Assembled Peptide Nanotubes
Author(s) -
Ghadiri M. Reza,
Kobayashi Kenji,
Granja Juan R.,
Chadha Raj K.,
McRee Duncan E.
Publication year - 1995
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199500931
Subject(s) - antiparallel (mathematics) , hydrogen bond , amphiphile , peptide , self assembly , nanostructure , materials science , beta sheet , molecular dynamics , superlattice , nanotechnology , chemistry , chemical physics , crystallography , computational chemistry , molecule , organic chemistry , copolymer , polymer , biochemistry , physics , quantum mechanics , magnetic field , optoelectronics , composite material
Nanostructures through self‐assembly: Suitably designed planar cyclic peptides like 1 form cylindrical dimers in nonpolar organic solvents. These ensembles are good models for the fundamental description of parallel and antiparallel β‐sheet structures as well as for the design of novel peptide nanostructures. The analysis of the structural and thermodynamic aspects of the dimerization process showed that the hydrogen bonds between the peptide backbones are crucial factors for the stability of the ensembles and selective formation of β‐sheet arrangements. Furthermore 1 crystallizes to form a novel, porous, solid‐state object with an amphiphilic tubular superlattice, which may have potential utility in the molecular inclusion of hydrophilic and hydrophobic substrates.