Epítómapapping

Epítómapapping, also known as **epitope mapping**, is a scientific technique used in immunology and biochemistry to identify and characterize specific regions of a protein, known as epitopes, that are recognized by antibodies. These epitopes are critical for understanding immune responses, vaccine development, and the design of therapeutic antibodies. The process involves systematically analyzing protein sequences or structures to pinpoint the exact amino acid residues that interact with antibodies or other immune system components.

The method typically begins with the generation of overlapping peptide libraries derived from the protein of interest. These peptides are then screened using various assays, such as enzyme-linked immunosorbent assays (ELISAs), surface plasmon resonance (SPR), or peptide microarray technology, to detect antibody binding. Advanced computational tools and algorithms may also be employed to predict potential epitopes based on sequence or structural data, though experimental validation remains essential.

Epitope mapping is widely applied in vaccine research, where it helps identify protective antigens and optimize immunogen design. It is also used in autoimmune disease studies to uncover self-reactive epitopes and in drug development to assess antibody-drug interactions. The technique has evolved with technological advancements, enabling higher throughput and greater precision in identifying linear and conformational epitopes—those that depend on the protein’s three-dimensional structure.

Despite its utility, epitope mapping presents challenges, including the complexity of conformational epitopes and the variability of immune responses among individuals. Nevertheless, it remains a cornerstone in immunology, bridging the gap between protein structure and immune function.