ABSTRACT
In recent years, near-infrared spectroscopy has developed into an analytical technique widely used in various fields. Because of its advantages of fast, green and non-destructive, it plays an increasingly prominent role in the field of traditional Chinese medicine (TCM) analysis. However, due to the complexity and overlap of spectra, near-infrared spectroscopy needs to be combined with chemometrics for analysis and calculation. The principle, application scope, advantages and limitations of near infrared spectroscopy and chemometrics are summarized in detail, in addition, their combined applications in the identification of the origin, authenticity, processed products, composition prediction and water content detection of TCM are reviewed. The authors discussed and analyzed the joint application of near-infrared spectroscopy and chemometrics in the field of TCM analysis, and summarized the unique advantages of the combined technology in the field of TCM, which had certain guiding significance for medical workers to better use this technology.
ABSTRACT
<p><b>OBJECTIVE</b>To study the molecular action mechanism of active constituents desoxyrhaponticin (DES) and human serum albumin (HSA).</p><p><b>METHOD</b>Under the simulated physiological condition, computer analog technology, fluorescent spectrometry and ultraviolet spectrum were combined to study the binding mechanism between drug and protein.</p><p><b>RESULT</b>Molecular modeling was adopted to establish the binding model between DES and HSA, suggesting that the interaction force maintaining drug and protein is mainly the hydrophobic interaction with a hydrogen-bond interaction. The results from spectroscopy indicated that the interaction between DES and HSA is a dynamic binding process with a high intensity. The value of the binding distance (r) between DES and HSA was low, which demonstrate the occurrence of energy transfer. DES made an impact on HSA' structural domain microcell conformation, which resulted in hydrophobic changes in binding areas. According to the fluorescent phase diagram technical analysis, the changes in the DES-HSA reaction conformational pattern showed a "two-state" model. According to the obtained thermodynamic parameters for the DES-HSA interaction, the interactional force between DES and HSA was mainly a hydrophobic interaction. The fluorescence polarization proved that a non-covalent compound was generated during the interaction between DES and HSA.</p><p><b>CONCLUSION</b>The spectrum experiment showed consistent results with the computer analog technology, which could provided certain reference for studies on the interaction between DES and HSA.</p>
Subject(s)
Humans , Models, Molecular , Protein Binding , Protein Conformation , Serum Albumin , Chemistry , Metabolism , Spectrometry, Fluorescence , Spectrophotometry, Ultraviolet , Stilbenes , Metabolism , ThermodynamicsABSTRACT
<p><b>OBJECTIVE</b>To analyze and compare molecular mechanisms of active ingredients of honeysuckle (chlorogenic acid, CGA) with bovine lactoferrin (BLF) or bovine serum albumin (BSA).</p><p><b>METHOD</b>The spectral experiment and the computer analog technology were combined to determine the binding parameters, energy transfer parameters and thermodynamic functions between CGA and proteins, study the molecular mechanism, and compare the differences in interactive mechanism between CGA and BLF or BSA.</p><p><b>RESULT</b>The interactive mechanism between CGA and BLF or BSA was a dynamic molecular mechanism, whereas the static quenching mechanism existed between the interaction of CGA and BSA, with differences in the bonding intensity due to difference temperature. The binding distance r between CGA and BLF/BSA was very short, indicating the phenomenon of energy transfer. The results of the molecular modeling showed that the main interaction force between CGA and BLF or BSA was hydrogen bonds, together with Van der Waals' forces and hydrophobic effect.</p><p><b>CONCLUSION</b>The computer analog shows consistent results with spectral experiment.</p>