Bound Water Molecules at the Interface between the HIV-1 Protease and a Potent Inhibitor, KNI-272, Determined by NMR

Solution conformations of KNI-272, a tri

Solution conformations of KNI-272, a tripeptide HIV protease inhibitor designed on the basis of substrate transition state: Determined by NMR spectroscopy and simulated annealing calculations

✍ Yasushi Ohno; Yoshiaki Kiso; Yuji Kobayashi 📂 Article 📅 1996 🏛 Elsevier Science 🌐 English ⚖ 543 KB

KNI-272, a highly selective and potent HIV protease inhibitor containing allophenylnorstatine [(2S,3S)-3-amino-2-hydroxy-4-phenylbutyric acid], named Apns, has been studied in dimethylsulfoxide-d6 by NMR spectroscopy and simulated annealing calculations. 1H and 13C spectra showed the presence of two