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关节软骨主成分的红外光谱学分析及表征 被引量:3

Fourier Transform Infrared Spectroscopic Analysis and Characterization of Principal Components of Articular Cartilage
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摘要 傅立叶变换红外光谱学(FTIRS)可以获得样品组成和结构的丰富信息,极大地提高了科学研究的效率并拓宽了研究领域。本文采用FTIRS研究软骨的主要组成成分(胶原蛋白和蛋白多糖PG)的红外光谱特征及相关适用性。通过对两种主成分的不同质量配比,分别检验红外各特征谱带(amide I,II,III和sugar位置带)的吸光度值,以及进行和质量相关的Lambert-Beer定律线性拟合与回归。吸光度值分别采用谱带的绝对高度、相对高度和积分面积三种方式表征,结果显示后两种吸光度表达方式更精确。此外还进一步发现在关节软骨和早期骨关节炎的研究中(PG和胶原蛋白质量相差不多)采用amide II(优于amide I)和sugar带分别定性或半定量地表征胶原蛋白和PG含量是有效可行的;而amide III位置带既不适合表征胶原蛋白也不适合表征PG的含量。这项研究为关节软骨和骨关节炎早期研究提供了更加快捷实用的方法,从而有利于早期骨关节炎的判断和修复监测。 Fourier transform infrared spectroscopy (FTIRS) that can obtain composition and structure information of samples greatly enhances the research efficiency and broadens re- search field. In this paper, FTIRS was employed to investigate the IR spectral characteristic and usability of principal components of articular cartilage, collagen and proteoglycan (PG). Three types of absorbance characterized by absolute height, relative height and integral area of each characteristic band were measured under the different quality ratio of collagen to PG. The dependences of characteristic band absorbance on collagen quality were fitted and regressed according to the Lambert-beer law. We found that the absorbances described by the relative height and integral area were more accurate than those by the absolute height when they were applied to represent collagen content. Additionally, amide II band, which is better than amide I band, and sugar band are suitable for qualitatively or semi-quantitatively characterizing collagen and PG content, respectively, in normal cartilage and osteoarthritis cartilage at early stage where PG content is close to that of collagen. The spectral bands at amide III location in cartil collagen or PG cont the investigation on age mixed with collagen and PG are not recommended to represent the ent in cartilage. This study will provide a simpler and quicker method for cartilage and early-stage osteoarthritis, which will be helpful for the diagnosis and recovery monitoring of early-stage osteoarthritis.
出处 《光散射学报》 北大核心 2014年第2期213-218,共6页 The Journal of Light Scattering
基金 国家自然科学基金(61378087) 南京航空航天大学引进人才科研启动基金(1003-56YAH13005) 高等学校博士学科点专项科研基金(20133218120017)
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参考文献17

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共引文献6

同被引文献46

  • 1Zheng Shaokuan, Xia Yang, Damages to the extracellular Bidthanapally A, et al matrix in articular carti lage due to cryopreservation by microscopic magnetic resonance imaging and biochemistry [J]. Magn Re- son Imaging, 2009, 27(5): 648-655.
  • 2Wilson W, Huyghe J M, van Donkelaar C C. Depth- dependent compressive equilibrium properties of ar- ticular cartilage explained by its composition [J]. Bi- omech Model Mechanobiol, 2007, 6(1/2): 43-53.
  • 3Chen S S, Faleovitz Y H, Schneiderman R, et al. Depth-dependent compressive properties of normal aged human femoral head articular cartilage: relation- ship to fixed charge density [J]. Osteoarthritis Carti- lage, 2001, 9(6): 561-569.
  • 4Xia Yang, Alhadlaq H, Ramakrishnan N, et al. Mo- lecular and morphological adaptations in compressed articular cartilage by polarized light microscopy and Fourier-transform infrared imaging [J]. Journal of Structural Biology, 2008, 164(1): 88-95.
  • 5Tan A H C, Mitra A K, Chang P C C, et al. As- sessment of blood-induced cartilage damage in rabbit knees using scanning electron microscopy [J]. J Or-thopaedic Surgery, 2004, 12(2):199-204.
  • 6Yin Jianhua, Xia Yang, Ramakrishnan N. Depth-de- pendent anisotropy of proteoglycan in articular carti- lage by Fourier transform Infrared Imaging[J]. Vi- brational Spectrosc, 2011, 57(2), 338-341.
  • 7Ramakrishnan N, Xia Yang, Bidthanapally A. Polar- ized IR microscopic imaging of articular cartilage [J]. Physics in Medicine and Biology, 2007, 52 (15) 4601-4614.
  • 8Camaeho N P, Torzilli P A, Mendelsohn R, et al. FTIR microscopic imaging of collagen and proteogly- can in bovine cartilage [J]. Biopolymers, 2001, 62 (1) : 1-8.
  • 9BiX, LiG, DotySB, etal. A novel method for de- termination of collagen orientation in cartilage by Fourier transform infrared imaging spectroscopy (FT-IRIS) [J]. Osteoarthritis Cartilage, 2005, ]3 (12) : 1050-1058.
  • 10Rieppo L, Narhi T, Helminen H J, et al. Infrared spec- troscopic analysis of human and bovine articular cartilage proteoglycans using carbohydrate peak or its second de- rivative[J]. J Biomed Opt, 2013, 18(9): 1-6.

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