Elastin-like polypeptides as models of intrinsically disordered proteins.
Elastin-like polypeptides (ELPs) are a class of stimuli-responsive biopolymers inspired by the intrinsically disordered domains of tropoelastin that are composed of repeats of the VPGXG pentapeptide motif, where X is a "guest residue". They undergo a reversible, thermally triggered lower critical solution temperature (LCST) phase transition, which has been utilized for a variety of applications including protein purification, affinity capture, immunoassays, and drug delivery. ELPs have been extensively studied as protein polymers and as biomaterials, but their relationship to other disordered proteins has heretofore not been established. The biophysical properties of ELPs that lend them their unique material behavior are similar to the properties of many intrinsically disordered proteins (IDP). Their low sequence complexity, phase behavior, and elastic properties make them an interesting "minimal" artificial IDP, and the study of ELPs can hence provide insights into the behavior of other more complex IDPs. Motivated by this emerging realization of the similarities between ELPs and IDPs, this review discusses the biophysical properties of ELPs, their biomedical utility, and their relationship to other disordered polypeptide sequences.
Duke University, Durham, NC, United States.
Stefan
S
Roberts
Duke University, Durham, NC, United States. Electronic address: mjd46@duke.edu.
Michael
M
Dzuricky
Duke University, Durham, NC, United States.
Ashutosh
A
Chilkoti
D000595:Amino Acid Sequence; D004549:Elastin / Q000737:chemistry*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D064267:Intrinsically Disordered Proteins / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D044366:Transition Temperature
D064267:Intrinsically Disordered Proteins; D010455:Peptides; D004549:Elastin
Biopolymer; Elastin-like polypeptide; Intrinsically disordered protein; Phase transition; Protein engineering; Tandem repeat