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Elastin‐Like Peptides (ELPs) – Building Blocks for Stimuli‐Responsive Self‐Assembled Materials
Author(s) -
Navon Yotam,
Bitton Ronit
Publication year - 2016
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.201500016
Subject(s) - pentapeptide repeat , chemistry , coacervate , elastin , residue (chemistry) , vesicle , micelle , peptide , amphiphile , biophysics , molecule , combinatorial chemistry , nanotechnology , polymer , biochemistry , organic chemistry , copolymer , membrane , medicine , materials science , pathology , aqueous solution , biology
Elastin‐like polypeptides (ELPs) are biopolymers composed of short repeating peptide motifs inspired by the native elastin hydrophobic domains, mostly the pentapeptide VPGXG, where X is a guest residue, which can be any amino acid except proline. The ability to control the hydrophobicity of ELPs, simply by changing the guest residue, and moreover, to transform an ELP from a soluble molecule to an insoluble one upon heating, makes them promising building blocks for novel stimuli‐responsive self‐assembled materials. Over the past decade, ELPs have been designed to self‐assemble into spherical and cylindrical micelles, fibres, vesicles, and coacervates. In this short review, we summarize the recent literature, describing the molecules and conditions employed to attain these desired structures.