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1. Self-Assembly of Stable Nanoscale Platelets from Designed Elastin-like Peptide–Collagen-like Peptide Bioconjugates

   https://doi.org/10.1021/acs.biomac.8b01681  

   Qin, Jingya ; Luo, Tianzhi ; Kiick, Kristi L. ( February 2019 , Biomacromolecules)
2. Microphase Separation of Resilin-like and Elastin-like Diblock Copolypeptides in Concentrated Solutions

   https://doi.org/10.1021/acs.biomac.1c00672  

   Navarro, Luis A. ; Ryan, Justin J. ; Dzuricky, Michael ; Gradzielski, Michael ; Chilkoti, Ashutosh ; Zauscher, Stefan ( September 2021 , Biomacromolecules)
3. Fabrication and Characterization of Recombinant Silk‐Elastin‐Like‐Protein (SELP) Fiber

   https://doi.org/10.1002/mabi.201800265  

   Roberts, Erin G. ; Rim, Nae‐Gyune ; Huang, Wenwen ; Tarakanova, Anna ; Yeo, Jingjie ; Buehler, Markus J. ; Kaplan, David L. ; Wong, Joyce Y. ( November 2018 , Macromolecular Bioscience)

   Silk‐elastin‐like‐protein polymers (SELPs) are genetically engineered recombinant protein sequences consisting of repeating units of silk‐like and elastin‐like blocks. By combining these entities, it is shown that both the characteristic strength of silk and the temperature‐dependent responsiveness of elastin can be leveraged to create an enhanced stimuli‐responsive material. It is hypothesized that SELP behavior can be influenced by varying the silk‐to‐elastin ratio. If the responsiveness of the material at different ratios is significantly different, this would allow for the design of materials with specific temperature‐based swelling and mechanical properties. This study demonstrates that SELP fiber properties can be controlled via a temperature transition dependent on the ratio of silk‐to‐elastin in the material. SELP fibers are experimentally wet spun from polymers with different ratios of silk‐to‐elastin and conditioned in either a below or above transition temperature (T_t) water bath prior to characterization. The fibers with higher elastin content showed more stimuli‐responsive behavior compared to the fibers with lower elastin content in the hot (57–60 °C) versus cold (4–7 °C) environment, both computationally and experimentally. This work builds a foundation for developing SELP materials with well‐characterized mechanical properties and responsive features.

    

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4. Grafting of short elastin-like peptides using an electric field

   https://doi.org/10.1038/s41598-022-21672-9  

   Pramounmat, Nuttanit ; Asaei, Sogol ; Hostert, Jacob D. ; Young, Kathleen ; von Recum, Horst A. ; Renner, Julie N. ( December 2022 , Scientific Reports)

   Abstract Surface-grafted elastin has found a wide range of uses such as sensing, tissue engineering and capture/release applications because of its ability to undergo stimuli-responsive phase transition. While various methods exist to control surface grafting in general, it is still difficult to control orientation as attachment occurs. This study investigates using an electric field as a new approach to control the surface-grafting of short elastin-like polypeptide (ELP). Characterization of ELP grafting to gold via quartz crystal microbalance with dissipation, atomic force microscopy and temperature ramping experiments revealed that the charge/hydrophobicity of the peptides, rearrangement kinetics and an applied electric field impacted the grafted morphology of ELP. Specifically, an ELP with a negative charge on the opposite end of the surface-binding moiety assembled in a more upright orientation, and a sufficient electric field pushed the charge away from the surface compared to when the same peptide was assembled in no electric field. In addition, this study demonstrated that assembling charged ELP in an applied electric field impacts transition behavior. Overall, this study reveals new strategies for achieving desirable and predictable surface properties of surface-bound ELP. 

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5. Facile formation of giant elastin-like polypeptide vesicles as synthetic cells

   https://doi.org/10.1039/D1CC05579H  

   Sharma, Bineet ; Ma, Yutao ; Hiraki, Harrison L ; Baker, Brendon M ; Ferguson, Andrew L ; Liu, Allen P ( December 2021 , Chemical Communications)

   We demonstrate the facile and robust generation of giant peptide vesicles by using an emulsion transfer method. These robust vesicles can sustain chemical and physical stresses. The peptide vesicles can host cell-free expression reactions by encapsulating essential ingredients. We show the incorporation of another cell-free expressed elastin-like polypeptide into the existing membrane of the peptide vesicles. 

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