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Arbitrary Self‐Assembly of Peptide Extracellular Microscopic Matrices
Author(s) -
Bella Angelo,
Ray Santanu,
Shaw Michael,
Ryadnov Maxim 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.201104647
Subject(s) - extracellular matrix , peptide , block (permutation group theory) , extracellular , biophysics , self assembly , matrix (chemical analysis) , chemistry , materials science , nanotechnology , biochemistry , biology , mathematics , combinatorics , chromatography
Two faces for one matrix : A single bifaceted cyclopeptide block forms highly branched, porous, and intricate fibrillar networks, which span microscopic dimensions and mimic the extracellular matrix to support cell growth and proliferation (see picture). The peptide block has two domains connected with triglycine linkers (GGG); the domains consist of positively (blue) and negatively (red) charged heptads that provide interactions between different blocks.