a 2013

LECTIN – CARBOHYDRATE INTERACTIONS DRIVEN BY DISPERSION

KOZMON, Stanislav, Michaela WIMMEROVÁ, Josef HOUSER, Radek MATUŠKA, Jaroslav KOČA et. al.

Základní údaje

Originální název

LECTIN – CARBOHYDRATE INTERACTIONS DRIVEN BY DISPERSION

Autoři

KOZMON, Stanislav (703 Slovensko, domácí), Michaela WIMMEROVÁ (203 Česká republika, domácí), Josef HOUSER (203 Česká republika, domácí), Radek MATUŠKA (203 Česká republika, domácí) a Jaroslav KOČA (203 Česká republika, garant, domácí)

Vydání

17th European Carbohydrate Symposium (EUROCARB 17), 2013

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10403 Physical chemistry

Stát vydavatele

Izrael

Utajení

není předmětem státního či obchodního tajemství

Kód RIV

RIV/00216224:14740/13:00072705

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

lectin; carbohydrate; dispersion interaction
Změněno: 20. 3. 2014 16:03, Mgr. Stanislav Kozmon, Ph.D.

Anotace

V originále

There are several ways how saccharides may interact with their receptors (e.g. classical hydrogen bonds, through metal ions as Ca(II)). The CH-pi interactions that occur between carbohydrates and aromatic amino-acids are also strongly involved in carbohydrate-recognition process. The strength and importance of the CH-pi carbohydrate-aromatic interaction is recently under heavy discussion among biomolecular scientists. Some of a recognition processes are performed by proteins called lectins, which are able to bind saccharides in a very specific way. In case of the RSL lectin, we have attempted for the first time to quantify how the CH/pi interaction contributes to an overall carbohydrate - protein interaction. We have used an experimental approach, creating single and double point mutants, combined with high level computational methods. Experimentally measured binding affinities were compared with computed carbohydrate-aromatic acid residue interaction energies. The AAL lectin is fucose-specific lectin with five structurally different binding sites for fucose moiety. Additionally, it has been discovered, that the AAL N224Q mutant structure exhibits interesting conformational flipping of incident Trp residue in two of the three binding sites that contain Trp side-chain. We aim to discover the nature of this Trp-flipping in mentioned binding sites. Therefore, we have attempted to analyze the impact of dispersion interaction to total binding potency also for AAL. Observed results suggest that in this and similar cases the carbohydrate-receptor interaction can be driven mainly by a dispersion interaction.

Návaznosti

CZ.1.05/1.1.00/02.0068, interní kód MU
Název: CEITEC - středoevropský technologický institut (Akronym: CEITEC)
Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC - středoevropský technologický institut, 1.1 Evropská centra excelence
2SGA2747, interní kód MU
Název: Saccharide - protein dispersion interactions involved in the bacterial recognition processes (Akronym: SaProDI)
Investor: Jihomoravský kraj, Saccharide - protein dispersion interactions involved in the bacterial recognition processes, Granty pro zahraniční vědce
286154, interní kód MU
Název: SYLICA - Synergies of Life and Material Sciences to Create a New Future (Akronym: SYLICA)
Investor: Evropská unie, SYLICA - Synergies of Life and Material Sciences to Create a New Future, Kapacity