Biomembranas formuojančių monosluoksnių ir adsorbuotų biomolekulių struktūros tyrimas virpesinės spektroskopijos metodais /

The structure and function of biomolecules are closely linked. Therefore, understanding processes that govern the changes in the molecular structure is of fundamental and practical importance. Here we analyze tethered bilayer lipid membranes (tBLM) and laccase enzymes at the electrode surface in water and controlled electric potential environments. Water is crucial in maintaining the native state of biomolecules, while the electric methods are widely used in studying such biomolecules. To realize how these forces affect the structure and orientation of surface-adsorbed tBLMs and laccase enzymes in-situ, we applied the surface-enhanced Raman spectroscopy (SERS). Anchoring monolayer is an integral part of tBLMs. Our data suggest that molecules in anchoring monolayer are prone to aggregate into hydrophobic clusters due to the water and/or electric potential in this way corrupting the functional properties of tBLMs. We also propose a conventional spectral indicator for the quality of the anchoring monolayer. The information on how the structure of surface-adsorbed enzymes is altered due to the changing external electric potential is still scarce. Presented in our study is the link between electrode potential and tertiary structure of the laccase enzymes and their functional properties. We show that at a negative potential enzymes adopt an extended-flat configuration, while at more positive electrode potential they acquire “native” vertical configuration and its activity.

Grantor dc:publisher

Institutional Repository of Vilnius University

Year dc:date

2020

Author dc:creator

• Talaikis, Martynas,

• Adsorption of biomolecules ; tethered bilayer lipid membrane ; laccase enzymes ; Raman spectroscopy

Statement dc:rights

• info:eu-repo/semantics/openAccess

Language dc:language

lit

Repository record dc:identifier

https://repository.vu.lt/VU:ELABAETD75724935&prefLang=en_US

OAI identifier oai:identifier

oai:vu.lt:elaba:75724935