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Morphology Diversity of L‐Phenylalanine‐Based Short Peptide Supramolecular Aggregates and Hydrogels
Author(s) -
MartíCentelles Rosa,
Escuder Beatriu
Publication year - 2018
Publication title -
chemnanomat
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.947
H-Index - 32
ISSN - 2199-692X
DOI - 10.1002/cnma.201800202
Subject(s) - self healing hydrogels , supramolecular chemistry , phenylalanine , peptide , morphology (biology) , alkyl , nanostructure , nanotechnology , chemistry , self assembly , materials science , biophysics , polymer chemistry , crystallography , organic chemistry , biochemistry , amino acid , crystal structure , biology , genetics
Supramolecular aggregates and hydrogels of diverse morphologies can be obtained by replacing the widely studied aromatic N‐capping of phenylalanine derivatives by long alkyl chains. Simple changes in chain length and number of phenylalanine residues lead to a diversity of nanostructures including networks of fibers of different handedness and flat nanosheets. Moreover, additional morphologies could be achieved by a simple pathway selection. These results evidence the impact that small structural and methodological changes have on the self‐assembly of small peptide fragments and recall its relevance for the understanding of protein aggregation as well as for the fine control of peptide material properties for applications.