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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.

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

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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