FP7Реинтеграция2012–2015

PRICE · Why and how do antifreeze proteins bind ice? An experimental study on the solution and adsorption behaviour of antifreeze proteins

7РП — „Хора“ (Действия „Мария Кюри“)

Период: 2012-01-01 → 2015-12-31
Финансиране от ЕС: 100 000 €
Участници: 1
Схема: MC-CIG

Линиите свързват координатора с партньорите.

Накратко на български

Протеините против замръзване при риби и насекоми се изследват, за да се разбере как те се прикрепят към ледените кристали и спират растежа им. Това помага за по-доброто разбиране на естествената защита на организмите срещу студа и намалянето на щетите от замръзване.

Този кратък обзор е генериран от изкуствен интелект

Кратко обяснение, генерирано от езиков модел по текста на CORDIS. Оригиналът е по-долу.

Резултати накратко

Why and how do antifreeze proteins bind ice? An experimental study on the solution and adsorption behaviour of antifreeze proteins.

Teaser Cold-adapted species of fish, insects and plants can survive in the harsh climate of the polar regions due to biological ‘antifreeze’ in the form of antifreeze proteins (AFPs). The AFPs ensure that the organisms remain unfrozen and therefore survive as the proteins stick to small ice crystals to inhibit further growth. Main text Polar fish remain unfrozen in shallow waters at subzero temperatures due to antifreeze proteins (AFPs) circulating in their blood, which reduce the freezing point of bodily fluids and block ice recrystallization. How this works is not yet fully understood, but adsorption of AFPs onto nascent ice crystals is thought to be of prime importance. The main aim of the PRICE project (entitled ‘Why and how do antifreeze proteins bind ice? An experimental study on the solution and adsorption behaviour of antifreeze proteins’) was to unravel the key mechanisms of action of AFPs. Researchers expressed and characterised type I and III AFPs in the laboratory. They achieved this using recombinant expression in Escherichia coli (HPLC-12 QAE type III AFP) bacteria and solid-phase peptide synthesis (HPLC-g type I AFP) following established protocols. The team further investigated the physico-chemical properties and activities of a wide variety of antifreeze proteins. Bulk association of several types of type I and III AFPs from winter flounder and ocean pout was studied using small-angle X-ray scattering. Furthermore, in collaboration with the Prof. Bakker laboratory at AMOLF in Amsterdam advanced spectroscopic tools were used to study the structure of the hydration layer and the solution structure of fish type III AFPs. The PRICE project advances our current understanding of the natural cryoprotective ability of AFPs which can help reduce freeze damage in various products and processes such as the cold preservation of organs and food products.

Текст от CORDIS, на английски · Данни: CORDIS, © Европейски съюз

Цел на проекта

Many Arctic and Antarctic species, including fish, insects, and plants, survive extreme cold byproducing antifreeze proteins (AFPs) that depress the freezing point of their bodily fluids in a non-colligative manner without altering its melting point. The ‘adsorption-inhibition mechanism’ has now been widely accepted to explain how AFPs achieve thermal hysteresis and inhibit ice recrystallisation, but why and exactly how AFPs bind ice is not yet known. This CIG project entitled ‘PRice’ entails an experimental study on antifreeze proteins in solution and at interfaces to identify and better understand key mechanisms by which AFPs function. The fundamental insights that we hope for are also of applied interest as the natural cryoprotective ability of AFPs can be very useful in the preservation of organs and food products upon freeze storage for example.The community contribution to PRice supports the integration of an excellent female researcher (MSc and PhD degrees were awarded with highest distinction) at an outstanding university in Europe. On March 1st 2011, she moved from the Adolphe Merkle Institute of the University of Fribourg in Switzerland to Eindhoven University of Technology (TU/e) in the Netherlands to take up a position as an Assistant Professor (6-year tenure track) within the Macromolecular and Organic Chemistry Group (MOC) of Prof. E. W. (Bert) Meijer and the Institute for Complex Molecular systems. She has an ideal background for this highly interdisciplinary project that will create new synergies between European research institutes and universities through collaborations between experimentalists of various nationalities and scientific backgrounds. The project will significantly advance her future career prospects as it opens up new possibilities to extend previous research activities and supports the establishment of her own subgroup within MOC at TU/e.

Оригинален текст от CORDIS (на английски).

Участници

TECHNISCHE UNIVERSITEIT EINDHOVEN · EindhovenКоординаторНидерландия