This study details the generation of an antibody-mediated osteoclast-targeting platform. This drug-delivery strategy may find utility as "a universal osteoclast-targeting platform" in order to directly target and deliver antiresorptive agents, anti-inflammatory agents, cathepsin K inhibitors, disintegrins, H + -ATPase inhibitors, and so on, directly to osteoclast cells. We have shown this platform is capable of being employed as an antiresorptive strategy, and our efforts will now center on the in vivo evaluation of this targeting strategy. Insights from Modeling the 3D Structure of New Delhi Metallo-β-Lactamse and Its Binding Interactions with Antibiotic Drugs New Delhi metallo-beta-lactamase (NDM-1) is an enzyme that makes bacteria resistant to a broad range of beta-lactam antibiotic drugs. This is because it can inactivate most beta-lactam antibiotic drugs by hydrolyzing them. For in-depth understanding of the hydrolysis mechanism, the three-dimensional structure of NDM-1 was developed. With such a structural frame, two enzyme-ligand complexes were derived by respectively docking Imipenem and Meropenem (two typical beta-lactam antibiotic drugs) to the NDM-1 receptor. It was revealed from the NDM-1/Imipenem complex that the antibiotic drug was hydrolyzed while sitting in a binding pocket of NDM-1 formed by nine residues. And for the case of NDM-1/Meropenem complex, the antibiotic drug was hydrolyzed in a binding pocket formed by twelve residues. All these constituent residues of the two binding pockets were explicitly defined and graphically labeled. It is anticipated that the findings reported here may provide useful insights for developing new antibiotic drugs to overcome the resistance problem. The rapid growth of antibiotic resistance has become a main clinical and epidemiological problem for human health [1] . In bacteria, b-lactam antibiotics are primarily hydrolyzed by blactamases in an acylation-deacylation-based process [2] . Thus, it is believed that b-lactamases play an important role in leading to resistance of bacteria to b-lactam antibiotics. These enzymes are capable of cleaving the amide bond of the b-lactam ring so as to inactivate the b-lactam antibiotic drugs. According to their sequence similarities, b-lactamases can be generally divided into four classes, named as A, B, C, and D. Classes A, C, and D of blactamases contain serine groups in their active sites, while the enzymes in class B are metalloproteins, or called ''metallo-blactamases'', that require one or two zinc ions for their activity. Among all the b-lactamases, metallo-b-lactamases are the major culprit causing bacteria to resist antibiotics, due to the reason that they can degrade all b-lactams except monobactams and that they are special for their constant and efficient carbapenemase activity [3] .