Bartosz Janusz

Abstract Understanding the pairing preferences and structural interactions between antibody heavy and light chains can enhance our ability to design more effective and specific therapeutic antibodies. Insights from natural antibody repertoires and conserved contact sites help reduce autoreactivity and improve drug safety and efficacy. Current databases represent only a limited portion of the estimated diversity of unique paired antibody molecules.

Abstract Antibodies are a cornerstone of the immune system, playing a pivotal role in identifying and neutralizing infections caused by bacteria, viruses, and other pathogens. Understanding their structure, and function, can provide insights into both the body's natural defenses and the principles behind many therapeutic interventions, including vaccines and antibody-based drugs.

Abstract Nanobodies are a subclass of immunoglobulins, whose binding site consists of only one peptide chain, bestowing favorable biophysical properties. Recently, the first nanobody therapy was approved, paving the way for further clinical applications of this antibody format. Further development of nanobody-based therapeutics could be streamlined by computational methods. One of such methods is infilling - positional prediction of biologically feasible mutations in nanobodies.