Petibois Cyril, Gouspillou Gilles, Wehbe Katia, Delage Jean-Paul, Déléris Gérard
CNRS UMR 5084, CNAB, Bio-Organic Chemistry Group, Université Victor Segalen Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux Cedex, France.
Anal Bioanal Chem. 2006 Dec;386(7-8):1961-6. doi: 10.1007/s00216-006-0828-0. Epub 2006 Oct 17.
Many muscular diseases result from abnormal organization of connective tissue and/or collagen network formation. Only a few molecular imaging techniques are able to analyze this collagen network by differentiating collagen types. In this study, FT-IR spectroscopy was used to analyze type I and IV collagens, the most important compounds of which are perimysium and endomysium, respectively. Secondary structure of collagen types was determined by curve-fitting the 1,700-1,480 cm(-1) spectral interval. Type I collagen could be differentiated from type IV by its higher amounts of triple helix and alpha-helix, but lower amounts of beta-sheets (P < 0.01). FT-IR imaging was then used to determine structural features of perimysium and endomysium collagen network in bovine Flexor carpi radialis muscle. Secondary structure of proteins contained in perimysium and endomysium was found to be very close to type I and IV collagens, respectively. FT-IR spectroscopy and imaging are thus analytical tools that might be used for investigating biodistribution and assembly of collagen types in connective tissues.
许多肌肉疾病是由结缔组织的异常组织和/或胶原网络形成引起的。只有少数分子成像技术能够通过区分胶原类型来分析这种胶原网络。在本研究中，傅里叶变换红外光谱（FT-IR）用于分析I型和IV型胶原，其最重要的成分分别是肌束膜和肌内膜。通过对1700-1480 cm(-1)光谱区间进行曲线拟合来确定胶原类型的二级结构。I型胶原与IV型胶原的区别在于，I型胶原的三螺旋和α-螺旋含量较高，而β-折叠含量较低（P < 0.01）。然后，利用FT-IR成像技术确定牛桡侧腕屈肌中肌束膜和肌内膜胶原网络的结构特征。发现肌束膜和肌内膜中所含蛋白质的二级结构分别与I型和IV型胶原非常接近。因此，FT-IR光谱和成像可能是用于研究结缔组织中胶原类型的生物分布和组装的分析工具。
