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Protein Affinity and Selectivity to Cellular Membranes

Project goals

Spatial and temporal organisation of proteins in cell is a crucial aspect for understanding the complex machinery of living cells. Peripheral proteins are organised at membranes of specific organelles to perform specialized functions. However, the relationship between the protein sequence and its membrane preference is not yet known. The aim of the proposed project is to identify, quantify, and explain protein affinity for membranes with specific composition and curvature. We will develop a computational method to determine the binding free energy of proteins and their mutants to specific membranes. The membranes to which we will design new peptides include human plasma membrane, membranes of organelles, virus envelopes, and tumor cells. We will focus on amphiphilic helices, a frequent membrane binding motif, and few selected complex proteins. Understanding the protein affinity to specific membranes will allow us to determine the preferred localization of proteins in cells and develop new protein biomarkers, sensors, scaffolds, and drugs.

Keywords

amphiphilic peptidephospholipid membranelipid compositionmolecular dynamicsalpha-helixaffinity

Public support

  • Provider

    Czech Science Foundation

  • Programme

    Standard projects

  • Call for proposals

    SGA0202000001

  • Main participants

    Masarykova univerzita / Středoevropský technologický institut

  • Contest type

    VS - Public tender

  • Contract ID

    20-20152S

Alternative language

  • Project name in Czech

    Proteinová přitažlivost a selektivita pro buněčné membrány

  • Annotation in Czech

    Prostorová a časová organizace proteinů v buňce je klíčovým aspektem pro pochopení komplexního mechanismu živých buněk. Periferní proteiny jsou organizovány na membránách specifických organel pro provádění specializovaných funkcí. Nicméně vztah mezi proteinovou sekvencí a její membránovou preferencí není dosud znám. Cílem navrhovaného projektu je identifikovat, kvantifikovat a vysvětlit proteinovou afinitu pro membrány se specifickým složením a zakřivením. Vyvineme výpočetní metodu pro stanovení vazebné volné energie proteinů a jejich mutantů na specifické membrány. Membrány, ke kterým budeme navrhovat nové peptidy, zahrnují lidskou plazmatickou membránu, membrány organel, virové obálky a nádorové buňky. Zaměříme se na amfifilní helixy, častý motiv pro interakci s membránami a několik vybraných komplexních proteinů. Pochopení afinity proteinu ke specifickým membránám nám umožní určit preferovanou lokalizaci proteinů v buňkách a vyvinout nové proteinové bioznačky, senzory, podpůrné konstrukce a léky.

Scientific branches

  • R&D category

    ZV - Basic research

  • OECD FORD - main branch

    10403 - Physical chemistry

  • OECD FORD - secondary branch

  • OECD FORD - another secondary branch

  • CF - Physical chemistry and theoretical chemistry

Completed project evaluation

  • Provider evaluation

    U - Uspěl podle zadání (s publikovanými či patentovanými výsledky atd.)

  • Project results evaluation

    The project was focused on protein attraction and selectivity for cell membranes. The results are clearly presented. A large number of students were involved in the project, several international collaborations were established. A total of 8 thematically focused works were published in very good journals. No deficiencies were found in compliance with the grant rules, including the use of funds.

Solution timeline

  • Realization period - beginning

    Jan 1, 2020

  • Realization period - end

    Dec 31, 2022

  • Project status

    U - Finished project

  • Latest support payment

    Apr 12, 2022

Data delivery to CEP

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

  • Data delivery code

    CEP23-GA0-GA-U

  • Data delivery date

    Jun 26, 2023

Finance

  • Total approved costs

    8,105 thou. CZK

  • Public financial support

    8,105 thou. CZK

  • Other public sources

    0 thou. CZK

  • Non public and foreign sources

    0 thou. CZK

Recognised costs

8 105 CZK thou.

Public support

8 105 CZK thou.

0%


Provider

Czech Science Foundation

OECD FORD

Physical chemistry

Solution period

01. 01. 2020 - 31. 12. 2022