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Table 1. Evaluation of the inhibition activity against HIV-1 integrase in both coupled andstrand transfer reactions of the two integramide A analogues and the natural compoundPeptideIC 50 for strandtransfer reactionIC 50 for coupledreactionnatural and synthetic integramide A 30-34 μM 7-10 μM[D-Iva 14 -L-Iva 15 ] integramide A 55 μM 8 μM[L-Pro 2,9,13 ] integramide A 60 μM 19 μM[L-Pro 2,9,13 , D-Iva 14 -L-Iva 15 ] integramide A 21 μM 10 μMFrom the results shown in Table 1, we can safely conclude that in general the two L-Procontainingintegramide A analogues are only slightly less active than natural (or synthetic)integramide A itself in inhibiting HIV-1 integrase.This study definitely confirms that the mixed α-/3 10 - helical conformation of naturalintegramide A plays a key role in its mechanism of inhibition. Moreover, our data provideevidence that the amphipathic character of this helical structure is not required for theactivity of integramide A against HIV-1 integrase. These observations will hopefully beuseful to further clarify the precise mechanism of inhibition of this interesting peptaib andto identify shorter peptide sequences active against HIV-1 integrase.References1. Singh, S.B., Hereth, K., Guan, Z., Zink, D.L., Dombrowski, A.W., Polishook, J.D., Silverman, K.C.,Lingham, R.B., Felock, P.J., Hazuda, D.J. Org. Lett. 4, 1431-1434 (2002).2. De Zotti, M., Damato, F., Formaggio, F., Crisma, M., Schievano, E., Mammi, S., Kaptein, B.,Broxterman, Q.B., Felock, P.J., Hazuda, D.J., Singh, S.B., Kirschbaum J., Brückner, H., Toniolo, C.Chem. Eur. J. 16, 316-327 (2010).293