BIOSILICA FORMATION · A Multi-Spectroscopic Investigation of Protein Structure in Biosilica Composites
7РП — „Хора“ (Действия „Мария Кюри“)
- Период
- 2012-09-01 → 2016-08-31
- Финансиране от ЕС
- 100 000 €
- Участници
- 1
- Схема
- MC-CIG
Линиите свързват координатора с партньорите.
Накратко на български
Молекулярните механизми, чрез които протеините контролират създаването на силициеви структури при диатомеите, се анализират чрез опростени пептидни модели. Разбирането на тези процеси помага да се разбере как природата синтезира наноструктури при стайна температура, за разлика от индустриалните методи.
Кратко обяснение, генерирано от езиков модел по текста на CORDIS. Оригиналът е по-долу.
Резултати накратко
A Multi-Spectroscopic Investigation of Protein Structure in Biosilica Composites
Proteins can fabricate hard and soft tissue. They sculpture the minerals in teeth and bone, shape cell membranes. While membrane proteins have been subject of significant research, the interaction of proteins with minerals are understudied. We know much less about the mechanisms involved in the formation of hydroxyapatide in teeth and bone and calcium carbonate in shells, mollusks and mussels. Within this project we have aimed at unraveling the molecular mechanisms involved in the silification of the cell walls of diatoms. These unicellular organisms are abundant in waters on earth and are the envy of material scientists because they can synthesize nanophase silica structures at room temperature in sea water ¬ – a process that takes material scientists extreme temperature and pHs. To better understand the fundamental principles behind the control proteins exert on biomineral structures, we chose to take a step forward and study simplified model peptides with reported control over mineral precipitation: a series of lysine-leucine peptides as well as a repeat unit of the diatom protein silafin. Our experiments based on sum frequency spectroscopy, solid state NMR, electron microscopy and simulations showed molecular details of the side chain-surface structure, interfacial folding and the resulting silica morphology in particles and nanometer thin films.
Текст от CORDIS, на английски · Данни: CORDIS, © Европейски съюз
Цел на проекта
We propose to use sum frequency generation (SFG), near edge X-ray absorption fine structure (NEXAFS) and solid state NMR spectroscopy to explore the structural basis for the control exerted by basic peptides on biosilica morphology. The long-term objective of this research is to elucidate the molecular recognition mechanisms used by proteins to control biomineralization processes. The questions we ask are: What is the structural basis for protein recognition of their native mineral phases? What structural motifs do proteins use to interact with mineral phases, and what amino acid side chains orient proteins at mineral interfaces? Answers to these questions would expand not only our understanding of the role played by proteins in biomineralization, but would also provide clear structure-based principles for the design of biomaterials and biomedical devices. However, due to the difficulties in studying protein structure and function at inorganic solid surfaces, there is still remarkably little known of the molecular structure-function relationships that govern hard tissue engineering by proteins. We know far less about the structures of proteins at biomineral interfaces than we know about the structures of membrane proteins. In this proposal we focus on protein regulation of biosilica morphology. It is widely recognized that proteins regulate formation of silica- based cell walls in diatoms. We propose to use a variety of spectroscopies that we have adapted for use in studying biomaterials, to determine how proteins direct the formation of silica-based nanospheres, nanotubules and other structures.
Оригинален текст от CORDIS (на английски).
Участници
- MAX-PLANCK-GESELLSCHAFT ZUR FORDERUNG DER WISSENSCHAFTEN EV · MUNCHENКоординаторГермания
Връзки
Данни: CORDIS, © Европейски съюз