ONLINE - Engineered Repeat Proteins in Nanobiotechnology: the examples of ELPs and CTPRs
CIC nanoGUNE Seminars
- Speaker
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Evangelos Georgilis, Self-Assembly Group
- When
-
2020/10/26
12:00 - Place
- nanoGUNE online Webinar
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**
**
**Engineered Repeat Proteins in Nanobiotechnology: the examples of ELPs and
CTPRs**
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Evangelos Georgilis
Self-Assembly Group, CIC nanoGUNE
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The use of recombinant DNA technology has led to the development of a wide
variety of artificial genes [1,2]. This has enabled the production of protein-
based polymers, known as recombinamers. Depending on their architecture,
recombinamers can be divided into intrinsically disordered [3] and structured
sequences [4].
An important example of disordered sequences are the elastin-like polypeptides
(ELPs), which find many applications in tissue engineering and nanomedicine
because of their biocompatibility and thermal response [5]. ELPs are comprised
of Val-Pro-Gly-Xaa-Gly pentapeptide repeats, where Xaa ≠Pro is the guest
residue. These polypeptides aggregate reversibly above a transition
temperature (Tt). By incorporating guest residues of different hydrophilicity,
it is possible to construct diblock ELPs which thermally assemble into
nanoparticles. The first part of this work is focused on my recent PhD project
in LCPO (Bordeaux), which had as a goal the development of diblock ELPs for
applications as thermoresponsive, self-assembled drug delivery vectors. A
series of diblock ELPs were designed, which were composed of an Ile-containing
hydrophobic block and a Met-containing block. This system could access
nanoparticle formation by chemoselective post-modifications of the Met
residue, as was shown by means of turbidimetry and light scattering.
On the other hand, the consensus tetratricopeptide repeat proteins (CTPRs)
represent a successful design of recombinamers with well-defined architectures
[6,7], which may serve to organize different elements in a distinct pattern.
CTPRs are comprised of a 34-residue motif folded into a pair of antiparallel
α-helices which self-assemble into elongated superhelices. The structural
integrity of these proteins renders them interesting candidates for
fabrication methods such as electrospinning, where the disruption of protein
structure may often occur [8]. The second part of this work is focused on my
current work on a joint project between nanoGUNE and biomaGUNE on electrospun
fibers of CTPRs. The characterization of these fibers by electron microscopy,
Raman spectroscopy and X-ray diffraction indicated the structural integrity of
CTPRs, therefore other elements may be precisely organized along the fiber
axis.
**References**
[1] J.C. RodrÃguez-Cabello, L. MartÃn, M. Alonso, F.J. Arias, A.M. Testera,
“Recombinamers†as advanced materials for the post-oil age, Polymer
(Guildf). 50 (2009) 5159–5169. doi:10.1016/j.polymer.2009.08.032.
[2] A. Girotti, A. Fernández-Colino, I.M. López, J.C. RodrÃguez-Cabello,
F.J. Arias, Elastin-like recombinamers: Biosynthetic strategies and
biotechnological applications, Biotechnol. J. 6 (2011) 1174–1186.
[3] K.M. Ruff, S. Roberts, A. Chilkoti, R. V. Pappu, Advances in Understanding
Stimulus-Responsive Phase Behavior of Intrinsically Disordered Protein
Polymers, J. Mol. Biol. 430 (2018) 4619–4635. doi:10.1016/j.jmb.2018.06.031.
[4] E.R.G. Main, A.R. Lowe, S.G.J. Mochrie, S.E. Jackson, L. Regan, A
recurring theme in protein engineering: The design, stability and folding of
repeat proteins, Curr. Opin. Struct. Biol. 15 (2005) 464–471.
doi:10.1016/j.sbi.2005.07.003.
[5] E. Georgilis, M. Abdelghani, J. Pille, E. Aydinlioglu, J.C.M. van Hest, S.
Lecommandoux, E. Garanger, Nanoparticles based on natural, engineered or
synthetic proteins and polypeptides for drug delivery applications, Int. J.
Pharm. 586 (2020). doi:10.1016/j.ijpharm.2020.119537.
[6] S.H. MejÃas, B. Sot, R. Guantes, A.L. Cortajarena, Controlled nanometric
fibers of self-assembled designed protein scaffolds, Nanoscale. 6 (2014)
10982–10988. doi:10.1039/c4nr01210k.
[7] T. Kajander, A.L. Cortajarena, E.R.G. Main, S.G.J. Mochrie, L. Regan, A
new folding paradigm for repeat proteins, J. Am. Chem. Soc. 127 (2005)
10188–10190. doi:10.1021/ja0524494.
[8] Y. Dror, T. Ziv, V. Makarov, H. Wolf, A. Admon, E. Zussman, Nanofibers
made of globular proteins, Biomacromolecules. 9 (2008) 2749–2754.
doi:10.1021/bm8005243.
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ONLINE seminar: Evangelos Georgilis; Self-Assembly Group - CIC nanoGUNE
When: Oct 26, 2020 11:00 AM Madrid
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