Bioinspired nanofilament coatings for scale reduction on steel.

Scaling of steel surfaces, prevalent in various industrial applications, results in significant operational inefficiencies and maintenance costs. Inspired by the natural hydrophobicity of springtail (Collembola) skin, which employs micro- and nanostructures to repel water, we investigate the application of silicone nanofilaments (SNFs) as a coating on steel surfaces to mitigate scaling. Silicone nanofilaments, previously successful on polymers, textiles, and glass, are explored for their hydrophobic properties and stability on steel.

Adhesion of the mucilage envelope of seeds probed by sum frequency generation spectroscopy.

The attachment of seeds to natural surfaces is important for the reproductive success of plants. This study investigates the adhesion mechanisms of seed mucilage to CaF and polystyrene surfaces, using sum frequency generation (SFG) vibrational spectroscopy and pull-off force measurements. The results show that the adhesion is driven by the formation of crystalline cellulose at the interface.

De Novo Design and Characterization of Amphiphilic Peptides with Basic Side Chains for Tailored Interfacial Chemistries.

Lysine-leucine (LK) peptides have been used as model systems and platforms for 2D material design for decades. LK peptides are amphiphilic sequences designed to bind and fold at hydrophobic surfaces through hydrophobic leucine side chains and hydrophilic lysine side chains extending into the aqueous subphase. The hydrophobic periodicity of the sequence dictates the secondary structure at the interface.

Estimation of vibrational spectra of Trp-cage protein from nonequilibrium metadynamics simulations.

The development of methods that allow a structural interpretation of linear and nonlinear vibrational spectra is of great importance, both for spectroscopy and for optimizing force field quality. The experimentally measured signals are ensemble averages over all accessible configurations, which complicates spectral calculations. To account for this, we present a recipe for calculating vibrational amide-I spectra of proteins based on metadynamics molecular dynamics simulations.

Investigating Lipase/Stain Interactions: Determining Interfacial Protein Conformation with Surface Spectroscopy.

Conventional bulk protein structure determination methods are not suitable for understanding the distinct and diverse interactions of proteins with interfaces. Notably, interfacial activation is a feature common to many lipases involving movement of a helical "lid" region upon contact with a hydrophobic surface to expose the catalytic site. Here we use the surface specificity of vibrational sum frequency generation spectroscopy (VSFG) spectroscopy to directly probe the conformation of lipase (TLL) at hydrophobic interfaces.

The secondary structure of diatom silaffin peptide R5 determined by two-dimensional infrared spectroscopy.

Diatoms, unicellular marine organisms, harness short peptide repeats of the protein silaffin to transform silicic acid into biosilica nanoparticles. This process has been a white whale for material scientists due to its potential in biomimetic applications, ranging from medical to microelectronic fields. Replicating diatom biosilicification will depend on a thorough understanding of the silaffin peptide structure during the reaction, yet existing models in the literature offer conflicting views on peptide folding during silicification.

Deep-Ultraviolet Photoexcitation of Aqueous Urea Forms Carbamic Acid/Carbamate in Less Than One Picosecond.

Urea is believed to have been essential to the synthesis of prebiotic nucleotides and thereby the RNA or DNA of the first lifeforms. Models suggesting that life began in wet-dry cycles around shallow aquatic ponds imply that reactants such as urea were exposed to deep ultraviolet irradiation from the young sun. Detrimental photodissociation of urea induced by deep UV excitation potentially challenges these models.

Probing Backbone Coupling within Hydrated Proteins with Two-Color 2D Infrared Spectroscopy.

The vibrational coupling between protein backbone modes and the role of water interactions are important topics in biomolecular spectroscopy. Our work reports the first study of the coupling between amide I and amide A modes within peptides and proteins with secondary structure and water contacts. We use two-color two-dimensional infrared (2D IR) spectroscopy and observe cross peaks between amide I and amide A modes.

Aqueous pyruvate partly dissociates under deep ultraviolet irradiation but is resilient to near ultraviolet excitation.

The deep ultraviolet photochemistry of aqueous pyruvate is believed to have been essential to the origin of life, and near ultraviolet excitation of pyruvate in aqueous aerosols is assumed to contribute significantly to the photochemistry of the Earth's atmosphere. However, the primary photochemistry of aqueous pyruvate is unknown. Here we study the susceptibility of aqueous pyruvate to photodissociation by deep ultraviolet and near ultraviolet irradiation with femtosecond spectroscopy supported by density functional theory calculations.

Two Receptor Binding Strategy of SARS-CoV-2 Is Mediated by Both the N-Terminal and Receptor-Binding Spike Domain.

It is not well understood why severe acute respiratory syndrome (SARS)-CoV-2 spreads much faster than other β-coronaviruses such as SARS-CoV and Middle East respiratory syndrome (MERS)-CoV. In a previous publication, we predicted the binding of the N-terminal domain (NTD) of SARS-CoV-2 spike to sialic acids (SAs). Here, we experimentally validate this interaction and present simulations that reveal a second possible interaction between SAs and the spike protein via a binding site located in the receptor-binding domain (RBD).

Umbrella-like Helical Structure of α-Synuclein at the Air-Water Interface Observed with Experimental and Theoretical Sum Frequency Generation Spectroscopy.

The misfolding of α-synuclein (αS) into amyloid aggregates is catalyzed by hydrophobic surfaces and associated with severe brain disorders, such as Parkinson's disease. Despite the important role of interfaces, the three-dimensional structure of αS at the interfaces is still not clear. We report interface-specific sum frequency generation (SFG) experiments of monomeric αS binding to the air-water interface, a model system for the important hydrophobic surfaces.

Peptide Orientation Strongly Affected by the Nanoparticle Size as Revealed by Sum Frequency Scattering Spectroscopy.

The orientation of proteins at interfaces has a profound effect on the function of proteins. For nanoparticles (NPs) in a biological environment, protein orientation determines the toxicity, function, and identity of the NP. Thus, understanding how proteins orientate at NP surfaces is a critical parameter in controlling NP biochemistry.

Elevated concentrations cause upright alpha-synuclein conformation at lipid interfaces.

The amyloid aggregation of α-synuclein (αS), related to Parkinson's disease, can be catalyzed by lipid membranes. Despite the importance of lipid surfaces, the 3D-structure and orientation of lipid-bound αS is still not known in detail. Here, we report interface-specific vibrational sum-frequency generation (VSFG) experiments that reveal how monomeric αS binds to an anionic lipid interface over a large range of αS-lipid ratios.

The primary photolysis of aqueous carbonate di-anions.

We study the primary photolysis dynamics of aqueous carbonate, CO(aq), and hydrogen carbonate, HCO(aq), when they are excited at = 200 nm. The photolysis is recorded with sub-picosecond time resolution using UV pump-Vis probe and UV pump-IR probe transient absorption spectroscopy and interpreted with the aid of density functional theory calculations. When CO is excited single photon absorption at = 200 nm, ( = 20 ps) = 82 ± 5% of the excited di-anions either detach an electron or dissociate.

Lysozyme Interaction with Phospholipid Nanodroplets Probed by Sum Frequency Scattering Vibrational Spectroscopy.

When a nanoparticle (NP) is introduced into a biological environment, its identity and interactions are immediately attributed to the dense layer of proteins that quickly covers the particle. The formation of this layer, dubbed the protein corona, is in general a combination of proteins interacting with the surface of the NP and a contest between other proteins for binding sites either at the surface of the NP or upon the dense layer. Despite the importance for surface engineering and drug development, the molecular mechanisms and structure behind interfacial biomolecule action have largely remained elusive.

Peptide Bond of Aqueous Dipeptides Is Resilient to Deep Ultraviolet Irradiation.

The susceptibility of aqueous dipeptides to photodissociation by deep ultraviolet irradiation is studied by femtosecond spectroscopy supported by density functional theory calculations. The primary photodynamics of the aqueous dipeptides of glycyl-glycine (gly-gly), alalyl-alanine (ala-ala), and glycyl-alanine (gly-ala) show that upon photoexcitation at a wavelength of 200 nm, about 10% of the excited dipeptides dissociate by decarboxylation within 100 ps, while the rest of the dipeptides return to their native ground state. Accordingly, the vast majority of the excited dipeptides withstand the deep ultraviolet excitation.

SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features.

Dynamin-like proteins are membrane remodeling GTPases with well-understood functions in eukaryotic cells. However, bacterial dynamin-like proteins are still poorly investigated. SynDLP, the dynamin-like protein of the cyanobacterium Synechocystis sp.

Periclase deforms more slowly than bridgmanite under mantle conditions.

Transport of heat from the interior of the Earth drives convection in the mantle, which involves the deformation of solid rocks over billions of years. The lower mantle of the Earth is mostly composed of iron-bearing bridgmanite MgSiO and approximately 25% volume periclase MgO (also with some iron). It is commonly accepted that ferropericlase is weaker than bridgmanite.

Orientation of the Dysferlin C2A Domain is Responsive to the Composition of Lipid Membranes.

Dysferlin is a 230 kD protein that plays a critical function in the active resealing of micron-sized injuries to the muscle sarcolemma by recruiting vesicles to patch the injured site via vesicle fusion. Muscular dystrophy is observed in humans when mutations disrupt this repair process or dysferlin is absent. While lipid binding by dysferlin's C2A domain (dysC2A) is considered fundamental to the membrane resealing process, the molecular mechanism of this interaction is not fully understood.

In Situ Identification of Secondary Structures in Unpurified Silk Fibrils Using Polarized Two-Dimensional Infrared Spectroscopy.

The mechanical properties of biomaterials are dictated by the interactions and conformations of their building blocks, typically proteins. Although the macroscopic behavior of biomaterials is widely studied, our understanding of the underlying molecular properties is generally limited. Among the noninvasive and label-free methods to investigate molecular structures, infrared spectroscopy is one of the most commonly used tools because the absorption bands of amide groups strongly depend on protein secondary structure.

Peptide Orientation at Emulsion Nanointerfaces Dramatically Different from Flat Surfaces.

The adsorption of protein to nanoparticles plays an important role in toxicity, food science, pharmaceutics, and biomaterial science. Understanding how proteins bind to nanophase surfaces is instrumental for understanding and, ultimately, controlling nanoparticle (NP) biochemistry. Techniques probing the adsorption of proteins at NP interfaces exist; however, these methods have been unable to determine the orientation and folding of proteins at these interfaces.

Broadband Multidimensional Spectroscopy Identifies the Amide II Vibrations in Silkworm Films.

We used two-dimensional infrared spectroscopy to disentangle the broad infrared band in the amide II vibrational regions of native silk films, identifying the single amide II modes and correlating them to specific secondary structure. Amide I and amide II modes have a strong vibrational coupling, which manifests as cross-peaks in 2D infrared spectra with frequencies determined by both the amide I and amide II frequencies of the same secondary structure. By cross referencing with well-known amide I assignments, we determined that the amide II (N-H) absorbs at around 1552 and at 1530 cm for helical and β-sheet structures, respectively.