PubMed · 4382806
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G Lowe. 1967-04-18. Possible hydrolytic mechanisms.. https://doi.org/10.1098/rspb.1967.0040
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Water from the solvent very strongly absorbs light in the frequency range of interest for studying protein structure by infrared (IR) spectroscopy. This renders handling of the observation cells painstaking and time consuming, and limits the reproducibility of the measurements when IR spectroscopy is applied to proteins in aqueous solutions. These difficulties are circumvented by the use of an Attenuated Total Reflectance (ATR) accessory. However, when protein solutions are studied, ATR spectroscopy suffers from several drawbacks, the most severe being nonproportionality of the observed absorbance with the protein concentration and spectral distortions that vary from protein to protein and from sample to sample. In this study, we show (1) that the nonproportionality is due to adsorption of the protein on the ATR crystal surface; (2) that the contribution of the crystal-adsorbed protein can easily be taken into account, rendering the corrected absorbance proportional to the protein concentration; (3) that the observed variable base line distortions, likely due to changes in the penetration depth of the light beam in solutions with the refractive index that depends on the protein concentration, can be easily eliminated; and (4) that ATR IR spectra thus corrected for protein adsorption and light penetration can be used to properly analyze the secondary structure of proteins in solution.
The interactions between tetracycline analogues (oxytetracycline, doxycycline, methacycline) and lysozyme (LYSO) were studied by using UV-visible absorption and spectrofluorimetric method. Tetracycline analogues can make LYSO's fluorescence quenching. The quenching mechanism is static quenching. Absorption spectrum and quenching constant all support this conclusion. The binding constants of tetracycline analogues with LYSO were obtained at various temperatures. According to the Förster nonradiative energy transfer theory, we can get the distances of donators and acceptors. We also determined the main acting force between them is electrostatic gravitation according to the thermodynamic parameter.
Synthetic peptides become more and more important as drug candidates in the treatment of a variety of diseases. A particular therapeutic focus for synthetic peptides is cancer treatment.1,2 In order to keep pace with the growing number of newly synthesized peptides, peptide purification should not represent the bottleneck in the drug discovery process. Since the target masses of synthetic peptides are well known, mass-based fraction collection represents an efficient technique for their purification. In contrast to fraction triggering with less specific detectors, employing a mass selective detector leads in each run only to the purification of the target mass. Consequently, it is not necessary to pick the compound of interest out of a series of redundant fractions. In this article we demonstrate mass-based purification of a variety of crude synthetic peptides by reversed phase high-performance liquid chromatography. The peptides were in the mass range from less than 1 kDa to more than 10 kDa and covered a pI range from 4 to 13. We particularly focused on some technical aspects of the system that were prerequisite for reliable compound purification with high recoveries.