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beta-Azidoalanine as an IR Probe: Application to a Monitoring of Local Electrostatic Environment in Amyloid Aggregates

2008년 8월 14일 18시 31분 14초
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목 <발표Ⅱ>
저자 및
오광임, 이주현, 조민행
고려대학교 화학과, Korea
beta-Azidoalanine dipeptide 1 was synthesized and its azido stretching vibrations in H2O and DMSO were studied by using Fourier transform (FT) IR spectroscopy. The dipole strength of the azido stretch mode is found to be about 19 and 5 times larger than those of CN and SCN stretch modes, respectively, which have been used as local environmental IR sensors. The azido stretch band in H2O is blue-shifted by about 14 cm−1 in comparison to that in DMSO, indicative of its sensitivity to electrostatic environment. To test the utility of beta-azidoalanine as an IR probe of local electrostatic environment in proteins, azidopeptide 4 was prepared by its incorporation into Abeta(16-22) peptide of the Alzheimer’s disease amyloid beta-protein at position Ala21. The amide I IR spectrum of 4 in D2O suggests that the azidopeptide thus modified forms in-register beta-sheets in aggregates as observed for normal Abeta(16-22). The azido peak frequency of 4 in aggregates is almost identical to that in DMSO, indicating that the azido group is not exposed to water but to hydrophobic environment. We believe that beta-azidoalanine will be used as an effective IR probe for providing site-specific information about the local electrostatic environments of proteins.