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DREAMY SIGNED

Disrupting Aberrant Protein–Protein Interactions with Conformationally Constrained Hydrocarbon α-Helical Mimetics

Total Cost €

0

EC-Contrib. €

0

Partnership

0

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 DREAMY project word cloud

Explore the words cloud of the DREAMY project. It provides you a very rough idea of what is the project "DREAMY" about.

positions    syn    preparation    avoidance    mcl    protrude    secondary    molecular    leucine    interface    peptidic    mechanics    theory    density    grace    chains    spectroscopy    aspartic    atoms    therapeutic    structure    replicate    defective    apoptosis    residues    substituted    faces    cover    critical    protein    interaction    14    anti    contiguously    mimetics    linear    dominated    chemistry    isoleucine    conformations    complete    edge    organic    controls    pattern    substituents    amino    computation    possibility    energy    18    arginine    benefit    divides    carbon    cancer    forms    disruption    host    small    ppi    cell    disease    merges    relative    nmr    configuration    explore    absolute    interactions    lives    many    competitive    noxa    area    active    positioning    synthetic    cutting    laboratory    alpha    saving    multiple    few    valine    helical    dynamics    usually    mediated    prepare    acid    molecule    11    ppis    alternating    dies    nature    owing    functional    12    pentane    fold    cells    16    uniquely    medicinal    certain    shallow    molecules    replacement    peptide    hotspot   

Project "DREAMY" data sheet

The following table provides information about the project.

Coordinator
UNIVERSITY OF BRISTOL 

Organization address
address: BEACON HOUSE QUEENS ROAD
city: BRISTOL
postcode: BS8 1QU
website: www.bristol.ac.uk

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country United Kingdom [UK]
 Total cost 195˙454 €
 EC max contribution 195˙454 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2017
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2018
 Duration (year-month-day) from 2018-10-10   to  2020-10-09

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    UNIVERSITY OF BRISTOL UK (BRISTOL) coordinator 195˙454.00

Map

 Project objective

Many critical processes within cells, including those that control whether a cell lives and divides or dies, are mediated by protein–protein interactions (PPIs). In certain disease states, such as cancer, these interactions can become defective in a way where disruption of the interaction has therapeutic benefit. Replacement of one of the protein partners, which often have α-helical secondary structure, with a small molecule is one method of disruption; however, the interface can often be large and shallow, making the design of competitive small molecules challenging. The saving grace is that the interaction energy is usually dominated by the interactions of a few amino acid residues, which protrude from one or more faces of the α-helical peptide. The design of α-helical mimetics that are non-peptidic in nature and that can replicate the positioning of these hotspot residues has been an active area of research. The host laboratory has recently developed a method to prepare chains of substituted carbon atoms with complete control of absolute and relative configuration. Owing to the avoidance of syn-pentane interactions, the all-syn and alternating syn–anti contiguously substituted chains fold into well-defined helical and linear conformations. The positioning of the substituents could uniquely replicate a pattern of hotspot residues that cover two or more faces of an α-helical peptide. This project will explore this possibility through the design, preparation and testing of mimetics that target the Mcl-1/Noxa-B PPI, which controls apoptosis and has leucine, arginine, isoleucine, aspartic acid, and valine at positions 11, 12, 14, 16 and 18 as hotspot residues. The project merges cutting-edge synthetic organic chemistry, multiple forms of computation, including molecular mechanics, density functional theory, and molecular dynamics, NMR spectroscopy, and medicinal chemistry.

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The information about "DREAMY" are provided by the European Opendata Portal: CORDIS opendata.

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