A key factor for successful design of bioactive complex, organic-inorganic hybrid biomaterials is the facilitation and control of adhesion at interfaces, as many current synthetic biomaterials are inert, lacking interfacial bio activity. In this regard, the development of a simple, unified way to bio functionalize diverse organic and inorganic materials toward biomineralization remains a critical challenge. In this report, a universal biomimetic mineralization route that can be applied to virtually any type and morphology of scaffold materials is provided to induce nucleation and growth of hydroxyapatite (HAp) crystals based on phase-transited lysozyme (PTL) coating. Surface-anchored abundant functional groups in the PTL enrich the interface with strongly bonded calcium ions, facilitating the formation of HAp crystals in simulated body fluid with the morphology and alignment being similar to that observed in natural HAp in mineralized tissues. By the adhesion of amyloid contained in the PTL, such protein assembly could readily integrate HAp on ceramics, metals, semiconductors, and synthetic polymers irrespective of their size and morphology, with robust bonding stability and corresponding ultralow wear extent under normal bone pressure. This strategy successfully improves the in vivo osteoconductivity of Ti-based implant, underpinning the expectation for such biomaterial in future biointerface and tissue engineering.

The design and scalable construction of robust ultrathin protein membranes with tunable separation properties remain a key challenge in chemistry and materials science. Here, we report a macroscopic ultrathin protein membrane with the potential for scaled-up fabrication and excellent separation efficiency. This membrane, which is formed by fast amyloid-like lysozyme aggregation at air/water interface, has a controllable thickness that can be tuned to 30–250 nm and pores with a mean size that can be tailored from 1.8 to 3.2 nm by the protein concentration. This membrane can retain > 3 nm molecules and particles while permitting the transport of small molecules at a rate that is 1~4 orders of magnitude faster than the rate of existing materials. This membrane further exhibits excellent hemodialysis performance, especially for the removal of middle-molecular-weight uremic toxins, which is 5~6 times higher in the clearance per unit area than the typical literature values reported to date.

Macromolecular crystallization has many implications in biological and materials science. Similar to the crystallization of other molecules, macromolecular crystallization conventionally considers a critical nucleus, followed by crystallographic packing of macromolecules to drive further crystal growth. Herein, we discover a distinctive macromolecular crystallization pathway by developing the concept of a macromolecular mesocrystal. This nonclassical polymer crystallization occurs through the mesoscale self-assembly of (bio)macromolecular nanocrystals. The new concept for macromolecular crystallization presented herein is fundamental and relevant to many fields, including materials science, chemistry, biomimetics, nanoscience, and structural biology.

PEI)-assisted crosslinking with catechol moieties, which could further be used as a Janus platform to support the reduction and attachment of silver nanoparticles on the film surface. [7] Freestanding organicmetal 2D films have potential in many application fields, such as in sensing, surface-enhanced Raman scattering, catalytic reaction, near-infrared photothermal therapy, and biomedical areas. [8][9][10][11] Unfortunately, such films are fabricated via multiple, time-consuming steps; [11,12] in addition, the sacrifice of metal conductivity greatly limits the applications of these materials in the electrical device field. [2,13] Herein, we report a facile, environmentally friendly and bio-based redox system to merge metal nanoparticles under ambient conditions in an aqueous solution via protein bonding, which is distinctive from traditional welding of nanomaterials at high temperatures/ pressures. We discover that the silver nanoparticles from the in situ reduction of silver ammonium ions by glucose were bound by ultrathin amyloid-like β-sheet stacking of lysozyme to create a freestanding large-area (e.g., 400 cm 2 ) 2D silver film at the air/water interface with a purity up to 98%. We prove the great ability of this reaction system toward controlled synthesis of highly reflective and highly conductive silver films with elongation nearly 10 times higher than that of pure metal without protein bonding. These characteristics allow the protein-bound silver films to crucially participate in realistic applications, such as in strain/pressure sensors and artificial throats with ultrasensitive capability for stealth transmission of Morse code via the detection of minute finger tapping and for silent speech recording via the detection of tiny vibrations of the human throat, a result never reported before. No special equipment is necessary for this one-step method, and we further demonstrate that the bonding function of lysozyme is general to other proteins (e.g., albumin, α-amylase, collagen, keratin, and pepsin) and other metal films besides Ag (e.g., Au and Cu) are synthesized easily by this strategy.The protein assembler lysozyme, generally recognized as a safe material by the US Food and Drug Administration, is commercially available at low cost from egg white, body fluids of animals and plant cells. [14] Figure 1a schematically illustrates the synthetic procedures of a lysozyme-bound silver film. Lysozyme from egg white, Tollen's reagent, and d-glucoseThe welding and sintering of nanomaterials is usually achieved at high temperatures and high pressures. Here, it is found that merging of metal nanoparticles occurs under ambient conditions in an aqueous solution via protein bonding. It is discovered that the silver nanoparticles from the in situ reduction of silver ammonium ions by glucose undergo confined nucleation and growth and are bound by ultrathin amyloid-like β-sheet stacking of lysozyme. This merging of silver nanoparticles creates a freestanding large-area (e.g., 400 cm 2 ) 2D silver film at the air/water i...

There has been a great interest in the phospholipids (PL) found in dairy products because of their health and functional properties. In this study, a technology that was originally developed for egg yolk PL extraction was applied to whey protein phospholipid concentrate (WPPC). This method successfully precipitated the proteins present in WPPC and extracted the lipids with a renewable alcoholic solvent, ethanol. The effect of ethanol concentration, extraction temperature, and extraction number on the recovery of total lipid, total PL, and individual PL class was evaluated. The optimum processing conditions for a combined 5-stage sequential extraction for producing a PL-enriched lipid fraction were determined to be 70% ethanol at 70°C, and the total lipid recovery, total PL recovery, and PL content achieved were 40.7, 58.1, and 45.8%, respectively. A lipid fraction with high nutritional value (high content of sphingomyelin or phosphatidylserine) can also be obtained by adjusting extraction conditions and collecting specific fractions, although the yield may decrease. Overall, producing a PL-rich lipid fraction from WPPC using ethanol extraction is feasible and scalable, and different processing conditions can be used depending on the type of lipid product desired.