Elastin-like polypeptides revolutionize recombinant protein expression and their biomedical application.
Elastin-like polypeptides (ELPs) are highly biocompatible and exhibit a potentially highly useful property: that of a thermally responsive reversible phase transition. These characteristics make ELPs attractive for drug delivery, appealing as materials for tissue repair or engineering, and improve the efficiency with which recombinant proteins can be purified. ELP fusion proteins (referred to as ELPylation) inherit the reversible phase transition property. ELPylation technology recently has been extended to plant cells, and a number of plant-based expression systems have been evaluated for the production of ELPylated proteins. Here, we discuss recent developments in ELP technology and the substantial potential of ELPs for the deployment of transgenic plants as bioreactors to synthesize both biopharmaceuticals and industrial proteins.
Floss
Doreen M
DM
Institute of Biochemistry, Christian-Albrechts-University, Olshausenstrasse 40, D-24098 Kiel, Germany.
Schallau
Kai
K
Rose-John
Stefan
S
Conrad
Udo
U
Scheller
Jürgen
J
D001672:Biocompatible Materials / Q000302:isolation & purification* / Q000378:metabolism; D004337:Drug Carriers / Q000302:isolation & purification* / Q000378:metabolism; D004549:Elastin / Q000096:biosynthesis / Q000302:isolation & purification*; D010452:Peptide Biosynthesis; D010455:Peptides / Q000302:isolation & purification*; D030821:Plants, Genetically Modified / Q000378:metabolism*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification*
D001672:Biocompatible Materials; D004337:Drug Carriers; D010455:Peptides; D011994:Recombinant Proteins; D004549:Elastin