title: Tunable self-assembly of genetically engineered silk--elastin-like protein polymers.
abstract: Silk--elastin-like protein polymers (SELPs), consisting of the repeating units of silk and elastin blocks, combine a set of outstanding physical and biological properties of silk and elastin. Because of the unique properties, SELPs have been widely fabricated into various materials for the applications in drug delivery and tissue engineering. However, little is known about the fundamental self-assembly characteristics of these remarkable polymers. Here we propose a two-step self-assembly process of SELPs in aqueous solution for the first time and report the importance of the ratio of silk-to-elastin blocks in a SELP's repeating unit on the assembly of the SELP. Through precise tuning of the ratio of silk to elastin, various structures including nanoparticles, hydrogels, and nanofibers could be generated either reversibly or irreversibly. This assembly process might provide opportunities to generate innovative smart materials for biosensors, tissue engineering, and drug delivery. Furthermore, the newly developed SELPs in this study may be potentially useful as biomaterials for controlled drug delivery and biomedical engineering.
authors.affiliation: Department of Biomedical Engineering, Tufts University, Medford, Massachusetts 02155, United States.
authors.forename: Xiao-Xia
authors.initials: XX
authors.lastname: Xia
authors.forename: Qiaobing
authors.initials: Q
authors.lastname: Xu
authors.forename: Xiao
authors.initials: X
authors.lastname: Hu
authors.forename: Guokui
authors.initials: G
authors.lastname: Qin
authors.forename: David L
authors.initials: DL
authors.lastname: Kaplan
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D004549:Elastin / Q000096:biosynthesis / Q000737:chemistry*; D004926:Escherichia coli; D018625:Microscopy, Atomic Force; D008855:Microscopy, Electron, Scanning; D008969:Molecular Sequence Data; D053758:Nanoparticles / Q000737:chemistry* / Q000648:ultrastructure; D010316:Particle Size; D055503:Protein Multimerization; D055550:Protein Stability; D020836:Protein Structure, Quaternary; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry*; D047011:Silk / Q000096:biosynthesis / Q000737:chemistry*
chemical_list: D011993:Recombinant Fusion Proteins; D047011:Silk; D004549:Elastin