DARKSIDE

Harnessing the Dark Side of Protein Folding: Manipulating Aggregation for Recombinant Protein Production

Coordinatore	THE HEBREW UNIVERSITY OF JERUSALEM.    more Spiacenti, non ci sono informazioni su questo coordinatore. Contattare Fabio per maggiori infomrazioni, grazie.
Nazionalità Coordinatore	Israel [IL]
Totale costo	1˙639˙400 €
EC contributo	1˙639˙400 €
Programma	FP7-IDEAS-ERC Specific programme: "Ideas" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
Code Call	ERC-2013-StG
Funding Scheme	ERC-SG
Anno di inizio	2013
Periodo (anno-mese-giorno)	2013-11-01   -   2018-10-31

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	THE HEBREW UNIVERSITY OF JERUSALEM.  Organization address address: GIVAT RAM CAMPUS city: JERUSALEM postcode: 91904 contact info Titolo: Dr. Nome: Daniel Cognome: Kaganovich Email: send email Telefono: +972 54 2462875 Fax: +972 722447007	IL (JERUSALEM)	hostInstitution	1˙639˙400.00
2	THE HEBREW UNIVERSITY OF JERUSALEM.  Organization address address: GIVAT RAM CAMPUS city: JERUSALEM postcode: 91904 contact info Titolo: Ms. Nome: Hani Cognome: Ben-Yehuda Email: send email Telefono: +972 2 6586676 Fax: +972 72 2447007	IL (JERUSALEM)	hostInstitution	1˙639˙400.00

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 Obiettivo del progetto (Objective)

'Nearly all desirable biological activities, whether for the purposes of nutrition, pharmacology, biofuel production, or waste disposal, can be carried out by proteins. Nature has furnished a vast array of bioactive and biocatalytic tools, and with the advent of rational protein design nearly any imaginable bioactivity is at our fingertips. There is, therefore, a pressing need for cost-effective, safe, and easily scalable strategies for generating Recombinant Proteins (rProteins). The main bottleneck for mass-producing a whole host of valuable biologically active rProteins is the difficulty of recovering functional proteins from expression hosts.

This difficulty stems largely from the lack of sufficient know-how for manipulating protein biogenesis in the cell. The key component of protein biology, whether in the context of rProtein production or cell viability, is enabling a protein to achieve its proper folding state. Most proteins do not fold on their own – they require the assistance of a vast network of folding managers, or chaperones. The cellular chaperone machinery not only assists protein folding, it also carries out quality control, ensuring that proteins that are damaged or unable to fold for other reasons are properly disposed of through degradation or protective aggregation. The aim of this proposal is to understand the protein biosynthetic pathway in sufficient detail, so as to be able to manipulate its overall function. My eventual goal is to exert control over folding and aggregation in order to produce higher yields of functional rProteins in eukaryotes. The biotechnological strategy will consist of: 1. Manipulating aggregation to remove damaged endogenous proteins from the folding proteome, thus diverting more resources to the folding of rProteins; 2. Manipulating the allocation of cellular chaperone resources between folding, degradation, and aggregation; 3. Utilizing aggregates to produce substantially higher amounts of functional rProteins.'