Self-Assembling Multidomain Peptide Fibers with Aromatic Cores

Self-assembling multidomain peptides have been shown to have desirable properties, such as the ability to form hydrogels that rapidly recover following shear-thinning and the potential to be tailored by amino acid selection to vary their elasticity and encapsulate and deliver proteins and cells. Her...

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Bibliographic Details
Published in:Biomacromolecules 2013-05, Vol.14 (5), p.1370-1378
Main Authors: Bakota, Erica L, Sensoy, Ozge, Ozgur, Beytullah, Sayar, Mehmet, Hartgerink, Jeffrey D
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acid Substitution
Aminoacids, peptides. Hormones. Neuropeptides
Analytical, structural and metabolic biochemistry
Applied sciences
Biocompatible Materials - chemical synthesis
Biological and medical sciences
Elasticity
Exact sciences and technology
Fundamental and applied biological sciences. Psychology
Hydrogels - chemical synthesis
Hydrogen Bonding
Hydrophobic and Hydrophilic Interactions
Microscopy, Electron, Scanning
Molecular Dynamics Simulation
Molecular Sequence Data
Nanofibers - chemistry
Nanofibers - ultrastructure
Natural polymers
Peptides - chemical synthesis
Phenylalanine - chemistry
Physicochemistry of polymers
Protein Structure, Tertiary
Proteins
Rheology
Tissue Scaffolds
Tryptophan - chemistry
Tyrosine - chemistry
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Summary:Self-assembling multidomain peptides have been shown to have desirable properties, such as the ability to form hydrogels that rapidly recover following shear-thinning and the potential to be tailored by amino acid selection to vary their elasticity and encapsulate and deliver proteins and cells. Here we describe the effects of substitution of aliphatic hydrophobic amino acids in the central domain of the peptide for the aromatic amino acids phenylalanine, tyrosine, and tryptophan. While the basic nanofibrous morphology is retained in all cases, selection of the particular core residues results in switching from antiparallel hydrogen bonding to parallel hydrogen bonding in addition to changes in nanofiber morphology and in hydrogel rheological properties. Peptide nanofiber assemblies are investigated by circular dichroism polarimetry, infrared spectroscopy, atomic force microscopy, transmission and scanning electron microscopy, oscillatory rheology, and molecular dynamics simulations. Results from this study will aid in designing next generation cell scaffolding materials.
ISSN:1525-7797
1526-4602
DOI:10.1021/bm4000019