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Remodeling Cross‐β Nanotube Surfaces with Peptide/Lipid Chimeras
Author(s) -
Ni Rong,
Childers W. Seth,
Hardcastle Kenneth I.,
Mehta Anil K.,
Lynn David G.
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201201173
Subject(s) - peptide , amphiphile , nanotechnology , lysine , biophysics , nanotube , self assembly , materials science , chemistry , biochemistry , biology , carbon nanotube , amino acid , organic chemistry , copolymer , polymer
Between the sheets : A unique cross‐β‐peptide amphiphile assembly positions the acyl chain within the hydrophobic cross‐β laminate (see picture; acyl chain: red, peptide: gray, lysine: blue). The atomic‐level structure of the self‐assembled surface can also be systematically altered, opening the possibility to create a wide range of nanostructured biomaterials.