EVO-PBS

On the Chemical Evolution of Proto-Bioenergetic Systems

 Coordinatore UNIVERSITY OF LEEDS 

 Organization address address: WOODHOUSE LANE
city: LEEDS
postcode: LS2 9JT

contact info
Titolo: Mr.
Nome: Martin
Cognome: Hamilton
Email: send email
Telefono: +44 113 343 4090
Fax: +44 113 343 0949

 Nazionalità Coordinatore United Kingdom [UK]
 Totale costo 200˙371 €
 EC contributo 200˙371 €
 Programma FP7-PEOPLE
Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
 Code Call FP7-PEOPLE-2011-IIF
 Funding Scheme MC-IIF
 Anno di inizio 2013
 Periodo (anno-mese-giorno) 2013-10-01   -   2015-09-30

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    UNIVERSITY OF LEEDS

 Organization address address: WOODHOUSE LANE
city: LEEDS
postcode: LS2 9JT

contact info
Titolo: Mr.
Nome: Martin
Cognome: Hamilton
Email: send email
Telefono: +44 113 343 4090
Fax: +44 113 343 0949

UK (LEEDS) coordinator 200˙371.80

Mappa


 Word cloud

Esplora la "nuvola delle parole (Word Cloud) per avere un'idea di massima del progetto.

emerged    chemical    ability    peptide    chemicals    couple    abilities    primitive    amino    evolve    chemically    enzymes    then    hydrolysis    peptides    atpase       explore    prebiotic    ppi    polyphosphate    reactions    contemporary    libraries    atp   

 Obiettivo del progetto (Objective)

'Contemporary biochemistry exploits condensed polyphosphates (e.g.: adenosine triphosphate, ATP) to drive metabolic processes. However, it is unlikely that such molecules emerged a priori from an abiotic environment as their synthesis and use requires the presence of sophisticated & complex protein catalysts. We propose that more primitive P-based chemicals pre-dated ATP, chemicals which (i) emerged readily from prebiotic environments, (ii) were capable of performing valuable (in the context of an emerging living system) chemical reactions and (iii) had the ability to evolve chemically into peptide-catalysed polyphosphate-based systems more common to contemporary life.

We have identified a candidate P-based chemical pyrophosphite [PPi(III)] for which we have plausible prebiotic provenance. We will explore here the ability of PPi(III) to couple prebiotically available amino acids to peptides with potential value to an emerging system. We know that PPi(III) will couple glycine to diglycine but we intend here to explore the complete amino-acid coupling space using robotic, parallel processing, multi-well reader technology to probe PPi(III)-mediated di, tri and tetrapeptide formation. These libraries will then be examined, in a feed-back loop, for their abilities to catalyze the hydrolysis of PPi(III). The significance of this is that polypeptide catalyzed polyphosphate hydrolysis represents a primitive mimic for the activity of contemporary ATPase enzymes. We will then explore the ability of PPi(III) to evolve chemically into pyrophosphate [PPi(V)], a closer cousin to ATP, in the presence of PPi(III)-generated peptides and explore the abilities of the peptide libraries to accelerate chemical reactions of PPi(V). In this way, we aim to chart a chemical evolutionary pathway to peptide-activated P-based chemicals, the forerunners of ATPase enzymes, from plausibly prebiotic systems.'

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