LECTIN – CARBOHYDRATE INTERACTIONS DRIVEN BY DISPERSION

KOZMON, Stanislav, Michaela WIMMEROVÁ, Josef HOUSER, Radek MATUŠKA and Jaroslav KOČA. LECTIN – CARBOHYDRATE INTERACTIONS DRIVEN BY DISPERSION. In 17th European Carbohydrate Symposium (EUROCARB 17). 2013.

Basic information

• Original name: LECTIN – CARBOHYDRATE INTERACTIONS DRIVEN BY DISPERSION
• Authors: KOZMON, Stanislav (703 Slovakia, belonging to the institution), Michaela WIMMEROVÁ (203 Czech Republic, belonging to the institution), Josef HOUSER (203 Czech Republic, belonging to the institution), Radek MATUŠKA (203 Czech Republic, belonging to the institution) and Jaroslav KOČA (203 Czech Republic, guarantor, belonging to the institution).
• Edition: 17th European Carbohydrate Symposium (EUROCARB 17), 2013.

Other information

• Original language: English
• Type of outcome: Conference abstract
• Field of Study: 10403 Physical chemistry
• Country of publisher: Israel
• Confidentiality degree: is not subject to a state or trade secret
• RIV identification code: RIV/00216224:14740/13:00072705
• Organization unit: Central European Institute of Technology
• Keywords in English: lectin; carbohydrate; dispersion interaction

Abstract

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.

Links

• CZ.1.05/1.1.00/02.0068, interní kód MU: Name: CEITEC - středoevropský technologický institut (Acronym: CEITEC)

Investor: Ministry of Education, Youth and Sports of the CR, CEITEC - Central European Institute of Technology, 1.1 European Centres of Excellence

• 2SGA2747, interní kód MU: Name: Saccharide - protein dispersion interactions involved in the bacterial recognition processes (Acronym: SaProDI)

Investor: South-Moravian Region, Incoming grants

• 286154, interní kód MU: Name: SYLICA - Synergies of Life and Material Sciences to Create a New Future (Acronym: SYLICA)

Investor: European Union, Capacities