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The success of therapeutic monoclonal antibodies has sparked a growing interest in creating streamlined molecules that retain the tight and specific target binding, low toxicity and low immunogenicity of antibodies, but are faster to discover as well as easier and less expensive to manufacture. In addition, there is an interest in developing smaller target-binding proteins that may penetrate tissues faster, and that lack the Fc-mediated effector function, which is unnecessary in a simple antagonist of receptor—ligand interactions or in a delivery vehicle for a toxic payload.
The final objective for the next generation of target-binding therapeutic proteins is modularity: These considerations first led to the development of small engineered antibody fragments, including single-chain antibodies Huston et al. Engineered antibodies and 10 Fn3-based target-binding proteins in context. C Detailed comparison of three-dimensional structures of V H and of 10 Fn3, showing diversified loops [colored as in a and b ] and the disulfide bond in the V H domain black.
In an even further departure from natural antibodies, the drive for simplicity, modularity, ease of production and favorable biophysical properties has led to the invention of designed target-binding proteins, also known as engineered scaffolds and antibody mimics Binz and Pluckthun, ; Gebauer and Skerra, Designed binding proteins are relatively small, single-chain and single-domain proteins with engineered sequence diversity that allows high-affinity, specific binding to a wide range of target antigens.
They are highly stable, soluble and well expressed in microbial systems. They can be selected from in vitro -generated libraries in their final therapeutic format, ensuring a fast discovery process, and they can be linked to create multi-specific therapeutics. Owing to their small size, most therapeutic designed target-binding proteins need to be modified to avoid fast renal clearance. Popular examples of this approach are chemical modification such as PEGylation and genetic linkage to a protein domain that binds a component of plasma, such as human serum albumin Holt et al.
Adnectins, a family of designed proteins based on the framework of the 10th human fibronectin type III domain 10 Fn3; Fig. The 10th fibronectin type III domain was utilized as the starting point for the design of a family of target-binding proteins due to its structural similarity to antibody variable domains, suitability for modular assembly into multi-functional molecules, favorable biophysical properties and its abundance in human blood and extracellular matrix, which demonstrates that inherently this scaffold is not toxic or immunogenic.
Despite the lack of significant sequence homology, antibody variable domains and 10 Fn3 Main et al. As is illustrated in Fig. One structural difference between the two is that, whereas the two beta sheets in antibody domains are linked through a disulfide bridge, 10 Fn3 contains no disulfides or free cysteines Fig.
Another difference is that antibody variable domains are somewhat larger than 10 Fn3, with two more beta strands and an extra turn, which is not typically involved in antigen binding. Loops BC, DE and FG of 10 Fn3 are structurally analogous to the antibody complementarity-determining regions CDR H1, H2 and H3, respectively, and are thus the obvious candidates for diversification to generate artificial target-binding surfaces.
Sequence alignment of 10 Fn3 to other fibronectin type III domains reveals a divergence in loop sequence and length Dickinson et al. Whereas thermostability and solubility of 10 Fn3 can decrease once its loops are replaced to allow target binding, the extremely high stability of the wild type means that even destabilized variants can be sufficiently stable for therapeutic applications Parker et al.
In addition, several studies have demonstrated the utility of approaches based on in vitro selection and on directed engineering that can increase the stability of wild-type 10 Fn3 and its target-binding mutants Koide et al. Published selections of 10 Fn3-based target-binding proteins in chronological order of publication.
The peptide sequence shown in the top line marks the wild-type 10 Fn3 positions replaced by a mixture of residues; the second line defines the nature of diversification. Dissociation constant of the highest-affinity variant found in the selection. Diversified codons commonly used to encode any natural amino-acid residue. The seven N-terminal residues were deleted during library construction.
Another advantage of 10 Fn3-based target-binding proteins is that they are naturally well suited for multimerization to generate multi-functional binding molecules. In nature, 10 Fn3 is a component of fibronectin, a long, single-chain polypeptide comprised type I, II and III domains separated by short linkers, with limited interactions between adjacent domains Fig. A genetically linked string of Adnectins with different specificities closely mimics this natural arrangement and is thus likely to be compatible with independent folding, stability and function of the individual binding domains.
In contrast, antibody variable domains are parts of a more compact, three-dimensional structure, with extensive packing and functional inter-dependence between the variable light and heavy domains Fig.
The functional role of 10 Fn3 in human fibronectin, integrin binding, is mediated by the RGD tripeptide found in the FG loop Leahy et al. The steps that lead from human 10 Fn3 to therapeutic Adnectins include:.
In addition, detailed structural characterization of Adnectin-target complexes using X-ray crystallography continues to inform the discovery process, especially library design and optimization strategies. The two earliest 10 Fn3-based library designs, published by Koide et al. The Koide library diversified five residues in the BC loop and five residues in a shortened FG loop, whereas the Xu library diversified seven residues in the BC loop, four residues in the DE loop and 10 residues in the full-length FG loop.
In both cases, the diversified residues were encoded by a mixture of nucleotides that allowed any amino-acid residue to appear in any diversified position, with different amino acids represented at different frequencies due to the uneven redundancy of the genetic code.
Since the publication of the first 10 Fn3-based libraries, library design has increased in complexity and sophistication, both in the choice of residues to diversify and in the ratio of amino-acid residues allowed in each diversified position. Target-binding molecules with low nanomolar to picomolar affinity have been selected from libraries of between 10 7 and 10 13 different variants generated by the diversification of the three CDR-like loops of human 10 Fn3, BC, DE and FG, using phage, yeast or mRNA display.
In several of the studies, diversity in the loop length as well as in loop sequence appeared to have contributed to high affinity of selected variants Xu et al. The published crystal structures of maltose-binding protein in complex with cognate 10 Fn3 variants Koide et al.
Still, when outcomes from similar selections were compared, libraries with a broader side-chain diversity appeared to have an advantage. In two separate selections from libraries of similar design, a library that allowed nine different amino-acid residues but favored tyrosine, serine and glycine Gilbreth et al.
GoPro has long been a leader in capturing high-quality action videos, and the new GoPro Fusion camera has even more to offer. Its powerful dual-lens system is designed to be the ultimate capture device for compelling content, creating video in 5.
Steps include stitching together images from the two feeds, extracting the desired p view or the full 5. Even the newest PC systems can strain to complete those tasks if the software isn't optimized to share the load between the cores and the GPU.
Depending on the quality you stitch and application of stabilization and parallax correction using the D. With overlap and black space around the circular image projected onto the rectangular image sensor, the two feeds can combine into a 5. GoPro recommends identical Class 10 or higher memory cards, with a maximum capacity of GB per slot. Output codec options include H. There are several options for video resolution—5. Users can also choose between stereo or degree directional audio.
Clearly, users intending to produce and upload top-quality action videos want more than consumer-level specs to handle the raw video.
They'll need plenty of RAM, and big hard drives, too. Every minute of stitched CineForm footage at 5. Even still images in megapixel resolution take up plenty of room. Rendering speeds for a degree clip depend primarily on how powerful your PC is.
Users are taking it upon themselves to benchmark the software and report the results on social media. One user remarked that it took more than seven hours to process a five-minute 5.
Once they upgraded, the time was cut dramatically. Intel's Navarro noted that the relationship between GoPro and Intel has been developing for about ten years. We worked with GoPro to understand all phases of the work.
The software is now heavily multithreaded and vectorized because the tasks involved are very CPU-intensive; the latest Fusion software now also includes GPU optimization using Intel Quick Sync Video for decoding input videos. The teams regularly communicated, with GoPro seeking technical information on multicore processing and Intel providing specifications, training, and software assistance.
The coordination has paid off for GoPro—according to reports, from the alpha phase through final release, rendering speed increased significantly. Consumers benefit from these optimizations in many ways, including experiencing a faster user interface and witnessing real-time previsualization during rendering. To fully appreciate the optimizations, users should adhere to GoPro Fusion's recommended system requirements:.
Image stabilization for video recording refers to a family of techniques that reduce jitter while recording a moving image. Without compensating for pan and tilt, a visible frame-to-frame jitter can render the video unsuitable for sharing, so there are technologies implemented in the lens itself or in the optical path, before the sensor converts the image into digital information.
GoPro Fusion has standard gyro-based stabilization in the hardware, which ensures smooth source video and makes it possible to hold the camera at any angle. Inside GoPro Fusion Studio, digital image stabilization occurs as a post-processing step, after content is recorded. Product reviewers have been positive about this software feature. PC Magazine said Fusion Studio delivered "…footage that is incredibly smooth and steady. It even passed our torture test, delivering stable video when mounted to the vibrating hood of a farm tractor.
Other cameras we put to the same test … delivered noticeably shaky results. GoPro Fusion users have the ability to capture more video than they actually need, as the two offset cameras can pull in a degree image that is a round fish-eye view of everything captured below.
The typical "fish-eye" view of a portion of degree capture. Imagine a skateboarder setting up for a shoot in a park; rather than installing multiple cameras on tripods around the venue, a user could set the GoPro Fusion camera up on a tripod somewhere near the middle of the scene, then get coverage of much of the area, as shown below.
This would enable the user to perform tricks and stunts around the tripod, capturing the moves on both camera feeds.
Intel and GoPro* partner up to Optimize GoPro Fusion* Studio Software for Multicore CPUs and GPUs
AUTHORIZED REPRESENTATIVE OF THE SURE-BRIGHT™ PROFUSION X are elegantly designed and precision engineered with seven high-power LED. How long does Fusion Pro™ need to cure before it can be exposed to water? Fusion Pro develops its hardness in typical installation environments over seven . Question: Is Fusion Pro Grout really Stain-Proof™ and Color Perfect™? Answer: Yes. Typically, Fusion Pro needs seven days to dry before it can be exposed.