Surface-Enhanced Raman Scattering Studies of Human Transcriptional Coactivator p300
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- 作者：G. V. Pavan Kumar ; B. A. Ashok Reddy ; Mohammed Arif ; Tapas K. Kundu ; Chandrabhas Narayana
- 刊名：Journal of Physical Chemistry B
- 出版年：2006
- 出版时间：August 24, 2006
- 年：2006
- 卷：110
- 期：33
- 页码：16787 - 16792
- 全文大小：184K
- 年卷期：v.110,no.33(August 24, 2006)
- ISSN：1520-5207
文摘
We report for the first time the surface-enhanced Raman scattering (SERS) studies on p300, a large multidomaintranscriptional coactivator protein. Vibration spectral analysis has been performed in an attempt to understandthe structure of the p300 in the absence of its crystal structure. Strong Raman bands associated with amidesI-III have been observed in the protein spectra. This has been confirmed by performing SERS on deuteratedp300. We also observe Raman bands associated with the 
pha.gif" BORDER=0>-helix, tryptophan, phenylalanine, tyrosine, andhistidine. These bands will provide an ideal tool to study the drug-protein interactions in therapeutics usingSERS. We have successfully demonstrated the chloride ion effect on the SERS of p300. The Raman intensityincreases in the SERS spectra upon addition of chloride ion along with appearance of new modes. We havedeveloped a new method, namely, the "sandwich technique", which could be used to perform SERS experimentson proteins in dry conditions.
pha.gif" BORDER=0>-helix, tryptophan, phenylalanine, tyrosine, andhistidine. These bands will provide an ideal tool to study the drug-protein interactions in therapeutics usingSERS. We have successfully demonstrated the chloride ion effect on the SERS of p300. The Raman intensityincreases in the SERS spectra upon addition of chloride ion along with appearance of new modes. We havedeveloped a new method, namely, the "sandwich technique", which could be used to perform SERS experimentson proteins in dry conditions.