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      Elastin-like polypeptides as models of intrinsically disordered proteins.

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          Abstract

          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.

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          Author and article information

          Journal
          FEBS Lett.
          FEBS letters
          Elsevier BV
          1873-3468
          0014-5793
          Sep 14 2015
          : 589
          : 19 Pt A
          Affiliations
          [1 ] Duke University, Durham, NC, United States.
          [2 ] Duke University, Durham, NC, United States. Electronic address: mjd46@duke.edu.
          Article
          S0014-5793(15)00729-2 NIHMS720803
          10.1016/j.febslet.2015.08.029
          4599720
          26325592
          632190c1-1e9f-4bf3-acc8-fb0301821910
          History

          Biopolymer,Elastin-like polypeptide,Intrinsically disordered protein,Phase transition,Protein engineering,Tandem repeat

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