Effective, safe, and pharmacokinetically suitable drugs are urgently needed to curb the ongoing COVID-19 pandemic. The main protease or 3C-like protease (M^proor 3CL^pro) of SARS-CoV-2 is considered an important target to formulate potent drugs corresponding to its crucial role in virus replication and maturation in addition to its relatively conserved active site. Promising baseline data on the potency and safety of drugs targeting SARS-CoV-2 M^proare currently available. However, preclinical and clinical data on the pharmacokinetic profiles of these drugs are very limited. This review discusses the potency, safety, and pharmacokinetic profiles of potential inhibitors of SARS-CoV-2 M^proand forward directions on the development of future studies focusing on COVID-19 therapeutics.

The 2019–2020 winter was marked by the emergence of a new coronavirus (SARS-CoV-2) related disease (COVID-19), which started in Wuhan, China. Its high human-to-human transmission ability led to a worldwide spread within few weeks and has caused substantial human loss. Mechanical antiviral control approach, drug repositioning, and use of COVID-19 convalescent plasmas (CPs) were the first line strategies utilized to mitigate the viral spread, yet insufficient. The urgent need to contain this deadly pandemic has led searchers and pharmaceutical companies to develop vaccines. However, not all vaccines manufactured are safe. Besides, an alternative and effective treatment option for such an infectious disease would include pure anti-viral neutralizing monoclonal antibodies (NmAbs), which can block the virus at specific molecular targets from entering cells by inhibiting virus-cell structural complex formation, with more safety and efficiency than the CP. Indeed, there is a lot of molecular evidence about the protector effect and the use of molecular feature-based NmAbs as promising therapeutics to contain COVID-19. Thus, from the scientific publication database screening, we here retrieved antibody-related papers and summarized the repertory of characterized NmAbs against SARS-CoV-2, their molecular neutralization mechanisms, and their immunotherapeutic pros and cons. About 500 anti-SARS-CoV-2 NmAbs, characterized through competitive binding assays and neutralization efficacy, were reported at the writing time (January 2021). All NmAbs bind respectively to SARS-CoV-2 S and exhibit high molecular neutralizing effects against wild-type and/or pseudotyped virus. Overall, we defined six NmAb groups blocking SARS-CoV-2 through different molecular neutralization mechanisms, from which five potential neutralization sites on SARS-CoV-2 S protein are described. Therefore, more efforts are needed to develop NmAbs-based cocktails to mitigate COVID-19.

Nanobodies are small, single-domain antibodies that have emerged as a promising tool in cancer immunotherapy. These molecules can target specific antigens on cancer cells and trigger an immune response against them. In this mini-review article, we highlight the potential of nanobodies in cell-mediated immunotherapy for cancer treatment. We discuss the advantages of nanobodies over conventional antibodies, their ability to penetrate solid tumors, and their potential to enhance the efficacy of other immunotherapeutic agents. We also provide an overview of recent preclinical and clinical studies that have demonstrated the effectiveness of nanobody-based immunotherapy in various types of cancer.

Nanobodies, derived from the immune systems of camelids such as alpacas and llamas, represent a novel class of therapeutics with significant potential in fighting respiratory viral infections, such as SARS-CoV-2 and influenza. Nanobodies are small biomolecules that are highly stable and have unique binding features that allow for the effective neutralization of viral particles and inhibition of viral replication. This review highlights the advantages of nanobodies over traditional antibodies, including cost-effective production and enhanced specificity for target antigens. We discuss the mechanisms through which nanobodies block viral entry, their applications in diagnostics, and the methodologies for their development, such as phage display technology. Furthermore, we explore the efficacy of nanobodies in preclinical studies and their potential in clinical settings. As research progresses, structural optimization and the exploration of combination therapies may enhance their therapeutic efficacy, providing a promising approach for addressing global health challenges caused by emerging viral pathogens.

As the world continues to grapple with infectious diseases, scientists are constantly searching for effective ways to combat these deadly pathogens. One promising avenue of research is the use of nanobodies as neutralization agents. These small proteins, derived from camelid antibodies, have several unique advantages over traditional antibodies, including their small size. Nanobodies are much smaller than conventional antibodies, typically weighing in at around 15 kDa compared to the 150 kDa of a typical human antibody. This small size allows them to penetrate into tight spaces that larger molecules cannot reach, such as the crevices on the surface of viruses or bacteria. This makes them highly effective at neutralizing viruses by binding to and blocking their key functional sites. In this mini-review we discuss the construction approaches of nanobodies, and some methods to increase the half-life of nanobodies. Moreover, we discuss Nanobodies and their therapeutic potential for infectious agents.