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1.
Arch Gynecol Obstet ; 290(5): 943-6, 2014 Nov.
Article in English | MEDLINE | ID: mdl-24866887

ABSTRACT

PURPOSE: Study of the molecular variation in pre-eclampsia placenta based on micro-Raman spectroscopy. METHODS: Five pregnant women with pre-eclampsia from Nanfang hospital were selected as study group whose average age is 28.5 years and 38 ± 2 weeks gestation. The same period of healthy pregnant women, whose average age is 27.6 years and pregnant 39 ± 1 weeks, as control group (n = 5). The normal and pre-eclamptic placental tissues are detected by micro-Raman spectroscopy with the spectrum resolution of 1 cm(-1). RESULTS: We find that the protein structure of α-helix, ß-pleated sheet and ß-turn is overlying in pre-eclamptic placenta, which lead to a disorder of protein structure. The Raman peaks assigned to tryptophan indole ring and phenylalanine in pre-eclamptic placental tissue are more higher than that in normal tissue. CONCLUSIONS: Results suggest that the ordered structures of the main chain in protein molecules are reduced significantly, and the amino acid of side chains is damaged obviously. And a principal component analysis is used to classify the Raman spectra between normal and pre-eclamptic placental tissues. This study presents that Raman spectroscopy has a great potential on the mechanism research and diagnosis of placental lesions.


Subject(s)
Placenta/chemistry , Pre-Eclampsia/diagnosis , Pregnancy Proteins/genetics , Spectrum Analysis, Raman/methods , Adult , Case-Control Studies , Female , Genetic Variation , Gestational Age , Humans , Pregnancy , Pregnancy Proteins/metabolism , Principal Component Analysis
2.
Guang Pu Xue Yu Guang Pu Fen Xi ; 32(3): 800-4, 2012 Mar.
Article in Chinese | MEDLINE | ID: mdl-22582656

ABSTRACT

Second harmonic generation (SHG) is a second-order nonlinear optical process that has symmetry constraints confining signal to regions lacking a center of symmetry. Using SHG microscopy, a variety of tissue structures have noninvasively been imaged by virtue of intrinsic signal generated by structured proteins such as collagen fibrils in connective tissues or the actomyosin lattice of muscle cells. In biochemistry and structure biology, the high-level structures of DNA and protein macro-molecules are similar in constructing mechanism, although DNAs consist of deoxynucleotides and proteins of amino acid residues. The principal purpose of present work is to detect the SHG signal from different DNA samples by spectral imaging technology based on two-photon excited fluorescence (TPEF) and SHG. These DNA samples include the solution of genomic DNA and extracted nuclei, and cultured living cells. Results show that we can obtain the SHG signal from solution of genomic DNA and extracted nuclei in routine condition, but nothing from cultured cell nuclei. After adding a little of absolute ethanol (less than 5% by volume) in culture medium, the SHG signal is detectable in the interested region of nuclei. The findings suggest that the interaction between ethanol and DNA in living cell gives rise to the shift of molecular conformation, and this shift changes some nonlinear optical properties of DNA molecules.


Subject(s)
DNA, Neoplasm/chemistry , Microscopy , Spectrum Analysis , Humans
3.
Guang Pu Xue Yu Guang Pu Fen Xi ; 32(2): 383-5, 2012 Feb.
Article in Chinese | MEDLINE | ID: mdl-22512173

ABSTRACT

Raman spectroscopy was used to study the influence of ultraviolet-A(UV-A) radiation on collagen I. The Raman spectra of collagen I and that after 90 min UV-A radiation were reported. The results proved that irradiation with 90 min UV-A caused the change in the structures of collagen I. Intramolecular hydrogen bonds were broken, and the hydrogen bonding system was changed. The intensity of helix was decreased, while the intensity of the disordered conformation in proteins such as random coil was increased. Otherwise, the UV-A radiation influenced the hydroxylation of proline and the content of hydroxyproline was reduced. The changes caused by UV-A radiation could damage the triple helical structure of collagen I. It would lead to a series of changes, such as the destruction of collagen fibers during the photoaging of skin.


Subject(s)
Collagen , Ultraviolet Rays , Hydrogen Bonding , Hydroxylation , Proline , Protein Structure, Secondary , Proteins , Spectrum Analysis, Raman
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