Certain antibodies may be able to remove Alzheimer's plaques from the brain, according to new research carried about in mice. As much as 20 years before the symptoms of Alzheimer's set in, people with the disease begin to develop amyloid beta plaques that build up in the brain and, scientists believe, interfere with neural signals to cause cognitive and memory losses. But researchers at Washington University School of Medicine have developed an antibody that can remove the proteins these plaques are made of altogether, according to their new research. Several recent clinical trials have tried to use antibodies to target the plaques, but none have gotten past these trial phases, and many treatments have come with unsustainable side effects. The new approach may offer a way around these side effects and stop Alzheimer's plaques before its heart-breaking symptoms begin, the researchers hope.
Mass spectrometry is a crucial tool for the identification of proteins and other biomolecules in biological samples. In recent years, methods for measuring the mass of individual molecules have been reported, but these methods cannot follow the assembly of protein complexes in real time and are limited to relatively large protein complexes. On page 423 of this issue, Young et al. (1) use light scattering to detect and measure the mass of individual unlabeled biomolecules that they had adsorbed from solution to a glass surface. The method allows for the direct detection of proteins as they assemble into functional complexes or misfolded aggregates.
Proteins are the workhorses of biology. Designing new, stable proteins with functions desirable in biotechnology or biomedicine remains challenging. Jacobs et al. developed a computational method called SEWING that designs proteins using pieces of existing structures (see the Perspective by Netzer and Fleishman). The new proteins can contain structural features such as pockets or grooves that are required for function. The solved structures of two designed proteins agreed well with the design models.
In the never-ending war on insect pests, the widespread soil bacterium Bacillus thuringiensis (Bt) is one of the greatest heroes. Insecticidal crystalline (Cry) proteins and vegetative insecticidal proteins (Vips) from Bt are treasured for their effectiveness against some devastating pests and their safety for beneficial insects, wildlife, and people (1). Sprays containing Bt proteins have been used for more than 70 years and remain valuable in organic and conventional agriculture, forestry, and vector control (1). Crops genetically engineered to produce Bt proteins were introduced 20 years ago and quickly became a cornerstone of pest management. They have suppressed pest populations, reduced reliance on insecticide sprays, enhanced control by natural enemies, and increased farmer profits (2–4).
Disordered proteins often fold as they bind to a partner protein. Most methods to measure transition paths rely on monitoring a single distance, making it difficult to resolve complex pathways. Kim and Chung used fast three-color single-molecule Foster resonance energy transfer (FRET) to simultaneously probe distance changes between the two ends of an unfolded protein and between each end and a probe on the partner protein.