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Front Cover: Fibrous Aggregates of Short Peptides Containing Two Distinct Aromatic Amino Acid Residues (C&B 11/2019)
Author(s) -
Lipinski Wojciech,
Wasko Joanna,
Walczak Malgorzata,
Fraczyk Justyna,
Kaminski Zbigniew J.,
Galecki Krystian,
Draczynski Zbigniew,
Krucinska Izabella,
Kaminska Marta,
Kolesinska Beata
Publication year - 2019
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.201900591
Subject(s) - chemistry , front cover , biocompatibility , peptide , fibril , in vitro , biophysics , stereochemistry , cover (algebra) , biochemistry , organic chemistry , mechanical engineering , engineering , biology
Front Cover . The front cover shows schematically how nature can inspire scientists. Observing naturally occurring protein comprising a β‐sheet motif often present in amyloids fibrils, it is possible to design and obtain new peptide materials for various applications. The use of a self‐assembling process allows the synthesis of peptides/peptidic materials that are characterized by diverse mechanical, physico‐chemical and biological properties that can be used as scaffolds in regenerative medicine. The short aromatic peptides able to form highly ordered fibrous structures in self‐assembling processes were identified. All peptides materials formed under physiological conditions (pH 7.2, 37 °C) are stable in in vitro test conditions, they do not show cytotoxic effects on the endothelial cell line EA.hy 926. The required parameters of biocompatibility were fulfilled by H‐PheCysTrp‐OH, H‐PheCysTyr‐OH, H‐PheTyrMet‐OH, and H‐TrpTyr‐OH, as reported by W. Lipinski et al . in their full paper at 10.1002/cbdv.201900339.