Surface-enhanced Raman scattering studies of human transcriptional coactivator p300.
We report for the first time the surface-enhanced Raman scattering (SERS) studies on p300, a large multidomain transcriptional coactivator protein. Vibration spectral analysis has been performed in an attempt to understand the structure of the p300 in the absence of its crystal structure. Strong Raman bands associated with amides I-III have been observed in the protein spectra. This has been confirmed by performing SERS on deuterated p300. We also observe Raman bands associated with the alpha-helix, tryptophan, phenylalanine, tyrosine, and histidine. These bands will provide an ideal tool to study the drug-protein interactions in therapeutics using SERS. We have successfully demonstrated the chloride ion effect on the SERS of p300. The Raman intensity increases in the SERS spectra upon addition of chloride ion along with appearance of new modes. We have developed a new method, namely, the "sandwich technique", which could be used to perform SERS experiments on proteins in dry conditions.
Pavan Kumar
G V
GV
Light Scattering Laboratory, Chemistry and Physics of Materials Unit, and Transcription and Disease Laboratory, Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur P.O., Bangalore 560064, India.
Ashok Reddy
B A
BA
Arif
Mohammed
M
Kundu
Tapas K
TK
Narayana
Chandrabhas
C
D001665:Binding Sites; D002712:Chlorides / Q000737:chemistry; D005898:Glass / Q000737:chemistry; D006801:Humans; D053768:Metal Nanoparticles / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D012834:Silver / Q000737:chemistry*; D013059:Spectrum Analysis, Raman; D013499:Surface Properties; D014867:Water / Q000737:chemistry; D050880:p300-CBP Transcription Factors / Q000737:chemistry*
D002712:Chlorides; D014867:Water; D012834:Silver; D050880:p300-CBP Transcription Factors