title: Ordering recombinant silk-elastin-like nanofibers on the microscale.
abstract: Self-assembled peptide/polypeptide nanofibers are appealing building blocks for creating complex three-dimensional structures. However, ordering assembled peptide/polypeptide nanofibers into three-dimensional structures on the microscale remains challenging and often requires the employment of top-down approaches. We report that silk-elastin-like protein polymers self-assemble into nanofibers in physiologically relevant conditions, the assembled nanofibers further form fiber clusters on the microscale, and the nanofiber clusters eventually coalesce into three-dimensional structures with distinct nanoscale and microscale features. It is believed that the interplay between fiber growth and molecular diffusion leads to the ordering of the assembled silk-elastin-like nanofibers at the microscale.
authors.affiliation: Department of Aerospace and Mechanical Engineering, University of Arizona, Tucson, Arizona 85721, USA.
authors.forename: Like
authors.initials: L
authors.lastname: Zeng
authors.affiliation: Department of Aerospace and Mechanical Engineering, University of Arizona, Tucson, Arizona 85721, USA.
authors.forename: Weibing
authors.initials: W
authors.lastname: Teng
authors.affiliation: Department of Aerospace and Mechanical Engineering, University of Arizona, Tucson, Arizona 85721, USA.
authors.forename: Linan
authors.initials: L
authors.lastname: Jiang
authors.affiliation: Department of Aerospace and Mechanical Engineering, University of Arizona, Tucson, Arizona 85721, USA.
authors.forename: Joseph
authors.initials: J
authors.lastname: Cappello
authors.affiliation: Department of Aerospace and Mechanical Engineering, University of Arizona, Tucson, Arizona 85721, USA ; Biomedical Engineering IDP and Bio5 Institute, University of Arizona, Tucson, Arizona 85721, USA.
authors.forename: Xiaoyi
authors.initials: X
authors.lastname: Wu
references.citation: Angew Chem Int Ed Engl. 2010 Jun 7;49(25):4257-60
references.pmid: 20446331
references.citation: J Am Chem Soc. 2011 Feb 16;133(6):1745-7
references.pmid: 21247161
references.citation: Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6728-33
references.pmid: 10841570
references.citation: Biomacromolecules. 2009 Nov 9;10(11):3028-36
references.pmid: 19788307
references.citation: Chem Soc Rev. 2011 Sep;40(9):4563-77
references.pmid: 21629920
references.citation: J Control Release. 1998 Apr 30;53(1-3):105-17
references.pmid: 9741918
references.citation: Proc Natl Acad Sci U S A. 1997 Jul 22;94(15):7942-7
references.pmid: 9223292
references.citation: J Am Chem Soc. 2010 May 12;132(18):6306-8
references.pmid: 20397724
references.citation: Biomacromolecules. 2011 Nov 14;12(11):3844-50
references.pmid: 21955178
references.citation: Proc Natl Acad Sci U S A. 2007 Jun 26;104(26):10853-8
references.pmid: 17567757
references.citation: Langmuir. 2009 Nov 3;25(21):12682-6
references.pmid: 19803470
references.citation: Nat Biotechnol. 2003 Oct;21(10):1171-8
references.pmid: 14520402
references.citation: Appl Phys Lett. 2011 Jun 27;98(26):263702-2637023
references.pmid: 21918580
references.citation: J Am Chem Soc. 2008 Oct 15;130(41):13691-5
references.pmid: 18803383
references.citation: Biomacromolecules. 2010 Dec 13;11(12):3219-27
references.pmid: 21058633
references.citation: Proc Natl Acad Sci U S A. 2004 Feb 24;101(8):2287-92
references.pmid: 14983002