a 2013

Interactions of carbohydrates with biomolecules. Role of the CH/pi interactions

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

Základní údaje

Originální název

Interactions of carbohydrates with biomolecules. Role of the CH/pi interactions

Autoři

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

Vydání

22nd International Symposium on Glycoconjugates (2013), 2013

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10403 Physical chemistry

Stát vydavatele

Čína

Utajení

není předmětem státního či obchodního tajemství

Kód RIV

RIV/00216224:14740/13:00072707

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

lectin; carbohydrate; dispersion interaction
Změněno: 20. 3. 2014 16:58, Mgr. Stanislav Kozmon, Ph.D.

Anotace

V originále

Molecular recognition plays crucial role in many biological processes, such as bacteria-host identification. Some of these recognition processes are performed by proteins called lectins, which are able to bind saccharides in a very specific way. In our study we have focused on RSL lectin from world-wide distributed bacteria Ralstonia solanacearum causing lethal wilt in many agricultural crops and the AAL lectin from Aleuria aurantia. Both above mentioned bacteria interact with hosts through their lectins, binding predominantly L-fucose. In this paper, we are interested in the role of the CH/pi interaction in binding abilities of these two lectins. In the RSL lectin, we have attempted for the first time to quantify how the CH/pi interaction contributes to a overall carbohydrate - protein interaction. We have used an experimental approach, creating single and double point mutants, combined with high level computational methods. The structure contains three monomer units of the lectin with six almost identical binding sites, where three of them are intramonomeric and the other three are intermonomeric. Experimentally measured binding affinities were compared with computed carbohydrate-aromatic acid residue interaction energies. Experimental binding affinities for the RSL wild type, phenylalanine and alanine mutants were -8.5, -7.1 and -4.1 kcal.mol-1, respectively. These affinities agree with the computed dispersion interaction energy between the carbohydrate and aromatic amino acid residues for RSL the wild type and the phenylalanine mutant, with respective values of -8.8 and -7.9 kcal.mol-1, excluding the alanine mutant where the interaction energy was -0.9 kcal.mol-1. Molecular dynamics simulations show that discrepancy can be caused by creation of a new hydrogen bond between the alpha-L-Me-fucoside and RSL. 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