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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

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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.

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

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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