Resumen Objetivo: Estudiar la proteina Plasmodium falciparum Normocyte Binding Protein-1 (PfNBP-1), partiendo de un metodo de caracterizacion fisico-matematica desarrollado previamente para peptidos de alta union del merozoito de malaria al eritrocito. Materiales y metodos: Se tomaron 21 peptidos con tamano de 20 aminoacidos no sobrelapados de los cuales dos son de alta union, se cuantifico la frecuencia de aparicion de los 20 aminoacidos esenciales en cada posicion y se calculo la probabilidad, sumatoria de probabilidad y la entropia con el objetivo de diferenciar matematicamente los peptidos de alta y baja union. Posteriormente se calcularon los mismos valores para peptidos teoricos analogos, en los que fueron cambiados por glicinas los aminoacidos criticos confirmados experimentalmente. Resultados: Los peptidos de PfNBP-1 comprobados experimentalmente de alta union, presentaron valores de probabilidad, sumatoria de probabilidad y entropia ubicados dentro del macroestado de union y sus peptidos teoricos analogos presentaron resultados que se diferenciaban cada vez mas del macroestado de union a medida que se reemplazaban aminoacidos criticos por glicinas. En cuanto a las secuencias de no union de PfNBP-1, se encontro que los valores calculados son diferentes a los asociados al macroestado de union, comprobando que en el 100 % de casos estudiados es posible diferenciar los peptidos de no union y alta union matematicamente. Conclusiones: La probabilidad y la entropia permiten caracterizar adecuadamente los peptidos de alta union de PfNBP-1, y evidenciar el orden matematico subyacente al proceso de union de proteinas de malaria. Abstract Objective: To study the Plasmodium falciparum Normocyte Binding Protein-1 (PfNBP-1) based on a of physicalmathematical characterization method previously developed for high binding peptides of malaria merozoite to erythrocyte. Materials and methods: 21 non overlapped peptides with size of 20 amino acids, including two of high binding were taken; the frequency of occurrence of the 20 essential amino acids in each position was quantified and probability, summation of probability and entropy were calculated in order to mathematically differentiate high and low binding peptides. Later the same values were calculated for theoretical analogs peptides, where the critical amino acids confirmed experimentally were changed by glycine. Results: The experimentally validated high binding peptides of PfNBP-1 showed values of probability, summation of probability and entropy located within the binding macrostate peptides and their theoretical analogues peptides presented results that differed increasingly of the binding macrostate as critical amino acids were replaced by glycine. For the PfNBP-1 sequences of non-binding, it was found that the calculated values are different from those associated with the macrostate of binding and it was verified that in 100% of studied cases it is possible to mathematically differentiate binding and non-binding peptides. Conclusions: The probability and entropy allow to adequately characterize the high-binding peptides of PfNBP-1 and show the mathematical order underlying the process of protein binding of malaria to the erythrocyte.