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Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli
Published on: June 9, 2014
Self-aggregation characteristics of recombinantly expressed human elastin polypeptides
C M Bellingham1, K A Woodhouse, P Robson
1Cardiovascular Research Program, Research Institute, Hospital for Sick Children, Toronto, ON, Canada.
Biochimica Et Biophysica Acta
|December 12, 2001
Summary
Specific sequences within hydrophobic domains are crucial for elastin self-assembly. This protein
Area of Science:
- Biochemistry
- Extracellular Matrix Biology
- Protein Self-Assembly
Background:
- Elastin, an extracellular matrix protein, provides extensibility and elastic recoil to tissues.
- Monomeric elastin can self-organize into fibrillar structures in vitro and in vivo.
- The role of specific hydrophobic and crosslinking domains in elastin self-assembly is not fully understood.
Purpose of the Study:
- To investigate the factors influencing elastin self-assembly using defined recombinant human elastin polypeptides.
- To determine the contribution of specific hydrophobic domains to elastin's self-organization propensity.
Main Methods:
- Utilized a series of defined, recombinant human elastin polypeptides.
- Measured coacervation temperature as an indicator of self-assembly propensity.
- Varied salt and polypeptide concentrations to assess their influence.
Main Results:
- Coacervation temperature was influenced by both salt and polypeptide concentrations.
- Hydrophobic domains were found to be essential for elastin polypeptide self-assembly.
- Molecular mass, number of hydrophobic domains, or general hydropathy did not fully explain coacervation temperature differences.
Conclusions:
- The specific sequences within hydrophobic domains are critical determinants of elastin polypeptide self-assembly.
- Elastin's self-organization is a complex process influenced by more than just the overall hydrophobicity or size of its domains.
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