Activation of nuclear factor kappa B (NFκB) leads to theinflammatory process. During this NFκB-dependent inflammationprocess, inducible nitric oxide synthase (iNOS) are expressedin the inflammatory cells. Our previous data indicated that aspecific septapeptide (GVAWWMY) from the soybean extractfermented by Bacillus licheniformis B1 inhibited iNOS mRNAexpression and NO production in cultured macrophage cells. Ourfurther experiments revealed that treatment of same septapeptideresulted in inhibition of LPS-induced NFκB activation byreversing degradation of IκBα, an inhibitory protein for NFκB. The molecular docking indicated that the septapeptide binds toIκB kinase β (IKKβ), and thus it can inhibit phosphorylation ofIκBα. Supporting this, the binding site for the septapeptide hasthe highest affinity (-8.7 kcal/mol) and the site was located atthe kinase domain (KD) of IKKβ, which can significantlyaffect the kinase activity of IKKβ.