Incorporation of short, charged peptide tags affects the temperature responsiveness of positively-charged elastin-like polypeptides

Elastin-like polypeptides (ELPs) are recombinant protein domains exhibiting lower critical solution temperature (LCST) behavior. This LCST behavior is controlled not only by intrinsic factors including amino acid composition and polypeptide chain length but also by non-ELP fusion domains. Here, we r...

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Bibliographic Details
Published in:Journal of materials chemistry. B, Materials for biology and medicine Materials for biology and medicine, 2019-09, Vol.7 (34), p.5245-5256
Main Authors: Lin, Charng-Yu, Liu, Julie C
Format: Article
Language:English
Subjects:
Affinity chromatography
Amino acid composition
Amino acid sequence
Composite materials
Elastin
Electrostatic properties
Epitopes
Fusion protein
Hydrophobicity
Incorporation
pH effects
Polymers
Polypeptides
Proteins
Salts
Sensitivity
Tags
Temperature effects
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Summary:Elastin-like polypeptides (ELPs) are recombinant protein domains exhibiting lower critical solution temperature (LCST) behavior. This LCST behavior is controlled not only by intrinsic factors including amino acid composition and polypeptide chain length but also by non-ELP fusion domains. Here, we report that the presence of a composite non-ELP sequence that includes both His and T7 tags or a short Ser-Lys-Gly-Pro-Gly (SKGPG) sequence can dramatically change the LCST behavior of a positively-charged ELP domain. Both the His and T7 tags have been widely used in recombinant protein design to enable affinity chromatography and serve as epitopes for protein detection. The SKGPG sequence has been used to improve the expression of ELPs. Both the composite tag and the SKGPG sequence are
ISSN:2050-750X
2050-7518
DOI:10.1039/c9tb00821g