TAILIEUCHUNG - Báo cáo khoa học: Structure and positioning comparison of two variants of penetratin in two different membrane mimicking systems by NMR

The Antennapedia homeodomain protein ofDrosophilahas the ability to penetrate biological membranes and the third helix of this protein, residues 43–58, known as penetratin (RQIKIWFQNRRMKWKK-amide) has the same trans-locating properties as the entire protein. The variant, RQI KIFFQNRRMKFKK-amide, here called penetratin (W48F,W56F) does not have the same ability. | Eur. J. Biochem. 270 3055-3063 2003 FEBS 2003 doi Structure and positioning comparison of two variants of penetratin in two different membrane mimicking systems by NMR Mattias Lindberg Henrik Biverstahl Astrid Graslund and Lena Maler Department of Biochemistry and Biophysics The Arrhenius Laboratories Stockholm University Sweden The Antennapedia homeodomain protein of Drosophila has the ability to penetrate biological membranes and the third helix of this protein residues 43-58 known as penetratin RQIKIWFQNRRMKWKK-amide has the same translocating properties as the entire protein. The variant RQI KIFFQNRRMKFKK-amide here called penetratin W48F W56F does not have the same ability. We have determined a solution structure of penetratin and investigated the position of both peptides in negatively charged bicelles. A helical structure is seen for residues Lys46 through Met54. The secondary structure of the variant penetra-tin W48F W56F in bicelles appears to be very similar. Paramagnetic spin-label studies and analysis of NOEs between penetratin and the phospholipids show that pene-tratin is located within the bicelle surface. Penetratin W48F W56F is also located inside the phospholipid bicelle however with its N-terminus more deeply inserted than that of wild-type penetratin. The subtle differences in the way the two peptides interact with a membrane in an equilibrium situation could be important for their translocating ability. As a comparison we have also investigated the secondary structure of penetratin W48F W56F in SDS micelles and the results show that the structure is very similar in SDS and bicelles. In contrast penetratin W48F W56F and penetra-tin appear to be located differently in SDS micelles. This clearly shows the importance of using realistic membrane mimetics for investigating peptide-membrane interactions. Keywords cell-penetrating peptide penetratin pAnt NMR bicelle. Cell-penetrating peptides CPPs have the ability to .

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