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Peptides with regularly alternating enantiomeric sequence: From ion channel models to bioinspired nanotechnological applications
Author(s) -
Novelli Federica,
De Santis Serena,
Morosetti Stefano,
Titubante Mattia,
Masci Giancarlo,
Scipioni Anita
Publication year - 2018
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.533
H-Index - 7
ISSN - 2475-8817
DOI - 10.1002/pep2.24043
Subject(s) - nanotechnology , peptide , enantiomer , sequence (biology) , molecule , combinatorial chemistry , amino acid , materials science , chemistry , stereochemistry , organic chemistry , biochemistry
Abstract Peptides are versatile building blocks that have been extensively used as peptide‐based organizers to generate bioinspired hybrid materials. Among them, those peptides characterized by regularly alternating enantiomeric sequences ( l , d ‐peptides) have attracted much interest. Their structures, which are not accessible to the corresponding homochiral peptides, have been exploited to achieve hybrid conjugates, the chemical and structural properties of which can be predetermined by correct design. Molecules that self‐assemble into hollow tubular architectures with side chains on the outer surface can form, allowing the introduction of new functionalities on amino acid residues containing reactive side chains. This provides an effective strategy to develop engineered nanotubes with the surface suitably tuned for applications in different fields, spanning from electronics to medicine.