Protein Handshake on the Nanoscale: How Albumin and Hemoglobin Self-Assemble into Nanohybrid Fibers
journal contributionposted on 03.01.2018, 00:00 by Christian Helbing, Tanja Deckert-Gaudig, Izabela Firkowska-Boden, Gang Wei, Volker Deckert, Klaus D. Jandt
Creating and establishing proof of hybrid protein nanofibers (hPNFs), i.e., PNFs that contain more than one protein, is a currently unsolved challenge in bioinspired materials science. Such hPNFs could serve as universal building blocks for the bottom-up preparation of functional materials with bespoke properties. Here, inspired by the protein assemblies occurring in nature, we introduce hPNFs created via a facile self-assembly route and composed of human serum albumin (HSA) and human hemoglobin (HGB) proteins. Our circular dichroism results shed light on the mechanism of the proteins’ self-assembly into hybrid nanofibers, which is driven by electrostatic/hydrophobic interactions between similar amino acid sequences (protein handshake) exposed to ethanol-triggered protein denaturation. Based on nanoscale characterization with tip-enhanced Raman spectroscopy (TERS) and immunogold labeling, our results demonstrate the existence and heterogenic nature of the hPNFs and reveal the high HSA/HGB composition ratio, which is attributed to the fast self-assembling kinetics of HSA. The self-assembled hPNFs with a high aspect ratio of over 100 can potentially serve as biocompatible units to create larger bioactive structures, devices, and sensors.
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self-assembling kineticsheterogenic natureHSAprotein nanofibersself-assembled hPNFsprotein assembliesprotein handshakebiocompatible unitstip-enhanced Raman spectroscopydichroism resultsbioactive structuresacid sequencesbuilding blocksProtein HandshakeHemoglobin Self-Assembleself-assembly routebottom-up preparationSuch hPNFsnanoscale characterizationTERSbioinspired materials scienceHGBaspect ratioethanol-triggered protein denaturationbespoke propertiesserum albuminNanohybrid Fibers