Dresden 2014 – wissenschaftliches Programm
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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 35: Biomaterials and Biopolymers (joint session with BP) I
CPP 35.5: Vortrag
Mittwoch, 2. April 2014, 16:15–16:30, ZEU 222
Elucidating insulin structure at hydrophobic interfaces — •Sergio Mauri1,2, Tobias Weidner2, and Heike Arnlods1 — 1Surface Science Research Centre, Department of Chemistry, University of Liverpool, UK — 2Max Planck Institute for Polymer Research, Mainz, Germany
Insulin unfolding and aggregation represents a hot topic for improving the delivery and storage of insulin based drugs.
Human insulin is a small peptide (51 amino acids) that regulates glycemia in the human body. It can be found in the form of hexamers, dimers and monomers: only the latter undergo unfolding and aggregation, forming fibril-like structures (amyloids).
It is generally known that interfaces trigger protein denaturation and eventually aggregation: in particular hydrophobic interfaces (such as the air/water interface) are known to disrupt insulin secondary structure, but the mechanism has not been explained in detail yet, since conventional spectroscopic methods do not have sufficient sensitivity to detect the interfacial protein layer.
Here we address this problem by applying a nonlinear optical technique, infrared-visible sum frequency generation, which is interface sensitive by virtue of optical selection rules and compare it to attenuated total internal reflection IR data at hydrophobic interfaces.