Application of a novel graph-theoretic folding degree index to the study of steroid-DB3 antibody binding affinity

A novel folding degree index, together with other macromolecular descriptors, is used to study steroid-DB3 antibody interactions. This index is based on graph spectral moments of a matrix representing the dihedral angles of a protein backbone. The causes influencing the different order of binding affinity of steroids to DB3 antibody are identified. It is shown that the changes in the chain compactness of the DB3 antibody with respect to its center of mass (radius of gyration) is compensated by a change in the folding degree index in the contrary sense. In fact, the increment in compactness of chain L and the lower increment in the folding degree index of chain IT are able to explain the variations in affinity for DB3 of the steroids studied. Consequently, the highest binding affinities are reached by increasing the compactness of chain L in DB3 at the same time that producing the smallest increment in the folding degree of chain H. This study shows the possibilities of application for the graph-theoretic folding degree index in studying drug-protein interactions. (C) 2002 Elsevier Science Ltd. All rights reserved.