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Secondary Structure Dependent Self‐Assembly of β‐Peptides into Nanosized Fibrils and Membranes
Author(s) -
Martinek Tamás A.,
Hetényi Anasztázia,
Fülöp Lívia,
Mándity István M.,
Tóth Gábor K.,
Dékány Imre,
Fülöp Ferenc
Publication year - 2006
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.200504158
Subject(s) - membrane , self assembly , helix (gastropod) , protein secondary structure , bundle , peptide , chemistry , crystallography , polymer science , beta sheet , nanotechnology , materials science , biochemistry , biology , composite material , ecology , snail
In control : The secondary structure dependent self‐assembly of β‐peptides in solution proves that natural biopolymers are not unique in their highly structured conformational behavior. Stereochemically controlled secondary structural units of β‐peptide strands and helices intrinsically self‐associate into pleated‐sheet sandwiches (see picture) and helix‐bundle membranes, respectively.