Journal of Nanomedicine & Nanotechnology

The self-assembling fungal protein Vmh2 as a versatile biointerface

11^th International Conference and Expo on Nanoscience and Molecular Nanotechnology

October 20-22, 2016 Rome, Italy

Paola Giardina, Alfredo Maria Gravagnuolo, Luca De Stefano, Jane Politi, Sara Longobardi, Paola Cicatiello, Eden Morales Narvaez and Arben Merkozi

University of Naples Federico II, Italy
Institute for Microelectronics and Microsystems-Naples National Research Council, Italy
Catalan Institute of Nanoscience and Nanotechnology, Spain

Posters & Accepted Abstracts: J Nanomed Nanotechnol

Abstract:

Biological interfacing of nanomaterials is crucial to improve their biocompatibility, dispersibility and selectivity towards various applications in the biotechnological and biomedical fields. Proteins are suitable candidates for the bioconjugation of nanomaterials and the amphiphilic proteins called hydrophobins have been reported to self-assemble into stable biofunctional coating on a wide variety of (nano) materials. Hydrophobins are fungal proteins whose functions are mainly based on their capability to self-assemble into amphiphilic films, adhering to several surfaces. Fibrillar structures formed by class I hydrophobins share many structural analogies with amyloid fibrils, such as stability and resistance to proteolysis. We have studied the class I hydrophobin produced by the edible Basidiomycetes fungus Pleurotus ostreatus, named Vmh2, and evaluated its self-assembly under an array of experimental conditions to define the key factors controlling the process. This protein has been exploited as interface on different materials (silicon, glass, gold, steel and 2D materials) to develop different biotechnological applications. As an example, a Vmh2 film formed on the steel sample plate of a MALDI-TOF mass spectrometer has been used to immobilize different enzymes involved in proteomic studies, providing a simple and rapid procedure for in situ serial digestions and analysis of protein sequences, including post-translational modifications. Moreover, we have set up the production of biofunctionalized defect-free graphene by using this hydrophobin. Due to the superior hydrophobicity and stability of this protein, we have obtained high concentrated graphene dispersions upon Vmh2 assisted exfoliation of raw graphitic material. Furthermore, controlled centrifugation enabled the selection of very stable, few-layer and defect-free graphene.

Biography :

Email: giardina@unina.it