G. P. Sachdev, A. Brownstein, J. Fruton
Jan 25, 1974
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Journal
The Journal of biological chemistry
Abstract
Abstract Several 9-peptidylaminoacridines have been synthesized, their spectroscopic properties have been examined, and studies have been performed by means of absorption and fluorescence spectrophotometry on their interaction with proteins (especially pepsin) and with DNA preparations. At pH 5, pepsin binds 9-(Phe-Phe-amino) acridine largely by virtue of the interaction of the Phe-Phe unit of the compound with the extended active site of the enzyme, the acridine portion being drawn into a region of lower polarity than that of the aqueous medium. The results obtained with pepsin are compared with those given by bovine serum albumin, α-chymotrypsin, and lysozyme. Although, at pH 5, 9-(Phe-Phe-amino)acridine appears to be bound by DNA preparations somewhat more tightly than is 9-acetylaminoacridine, the absorption and emission spectra of these acyl-aminoacridines are not altered by interaction with DNA to the extent seen with the 9-aminoacridinium cation under comparable experimental conditions.