"ONLINE - Rational design of self-assembling amyloid building blocks as scaffolds for novel biomaterials"

Who: Anna Mitraki; University of Crete

Place: nanoGUNE online webinar

Date: Monday, 17 May 2021, 11:00

Rational design of self-assembling amyloid building blocks as scaffolds for novel biomaterials


Prof. Anna Mitraki 

Professor, Department of Materials Science and Technology, University of Crete, and IESL/FORTH


Self-assembling peptides gain increasing interest as scaffolds for novel bionanomaterials; rationally designed self-assembling building blocks are especially attractive. We have been focusing on modular designs that consist of a central ultrashort amphiphilic motif derived from the adenovirus fiber shaft. This central amphiphilic motif can be further modified with amino acids targeted for various functionalities. We have been using a combination of computational (in collaboration with Prof. Phanourios Tamamis at Texas A& M University) and experimental approaches towards such rational self-assembling peptide designs [1]. The designer peptides self-assemble into fibrils that are structurally characterized with Transmission Electron Microscopy, Scanning Electron Microscopy and X-ray fiber diffraction; these fibrils were previously targeted to bind to metal nanoparticles, silica, calcium, and more recently, cells [2]. Recently, we demonstrated that self-assembling peptide sequences derived from HIV gp120 V3 loop sequences and amyloid beta peptide that comprise a central self-assembling beta sheet core, with suitable selected replacements at flexible positions can serve as designable scaffolds for amyloid-based materials [3]. On that basis, we designed and studied functional amyloid materials with cesium binding, deposition and capture properties [4]. More recently, the aforementioned peptide cores were further designed to contain positively charged and aromatic residues exposed at key exposed positions in order to additionally promote DNA condensation and cell internalization. The results demonstrate that these designer peptide fibrils can act as CPP (Cell-Penetrating Peptides), can efficiently enter mammalian cells while carrying packaged luciferase- encoding plasmid DNA and act as a protein expression enhancers. Interestingly, the peptides further exhibited strong antimicrobial activity against the enterobacterium Escherichia coli [5].


Such short self-assembling peptides that are amenable to computational design offer open-ended possibilities towards multifunctional bionanomaterial scaffolds of the future [6].



References 

1. Tamamis, P., Kasotakis, E. Archontis, G. and Mitraki, A. (2014) ?Combination of experimental and theoretical approaches for the design and study of fibril-forming peptides? in ?Protein design: Methods and applications, second edition? edited by Valentin Kohler, in Methods in Molecular Biology series, Humana Press, Springer Science, NY, 1216: 53-70

2. Deidda G.  et al., Self-assembled amyloid peptides with Arg-Gly-Asp (RGD) motifs as scaffolds for tissue engineering. ACS Biomaterials Sci. and Engineering 3, (2017), 1404-1416

3. Kokotidou C. et al., A Novel Amyloid Designable Scaffold and Potential Inhibitor Inspired by GAIIG of Amyloid Beta and the HIV-1 V3 loop. FEBS letters, (2018) 592 :1777-1788.

4. Jonnalagadda SVR et al., Computational design of functional amyloid materials with cesium binding, deposition and capture properties. J. Phys. Chem. B. (2018) 122:7555-7568 

5. Kokotidou C. et al., Designer Amyloid Cell-Penetrating Peptides for Potential Use as Gene Transfer Vehicles. (2020) Biomolecules 10 :7, DOI: 10.3390/biom10010007

6.  Kokotidou, C., Tamamis, P. & Mitraki, A.  (2020) ?Amyloid-like peptide aggregates? ?in ?Peptide-based Biomaterials? edited by Mustafa O. Guler, The Royal Society of Chemistry series, pp. 217-268.




Host: E. Georgelis



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ONLINE nanoGUNE: Anna Mitraki; University Crete - CIC nanoGUNE

When: May 17, 2021 11:00 AM 


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https://zoom.us/j/94555313571?pwd=MzJLRFZEU1hDK0hpODN0TC9pUEpwUT09

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