Arbitrary self-assembly of peptide extracellular microscopic matrices

Angelo Bella; Santanu Ray; Michael Shaw; Maxim G. Ryadnov

doi:10.1002/anie.201104647

Arbitrary self-assembly of peptide extracellular microscopic matrices

Angelo Bella, Santanu Ray, Michael Shaw, Maxim G. Ryadnov

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Pages (from-to)	428-431
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	51
Issue number	2
DOIs	https://doi.org/10.1002/anie.201104647
Publication status	Published - 9 Jan 2012

Keywords

cell adhesion
extracellular matrix
protein design
self-assembly
tissue engineering

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10.1002/anie.201104647

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Arbitrary self-assembly of peptide extracellular microscopic matrices

Abstract

Keywords

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