Articular Cartilage Infrared Spectrum Imaging And Analysis Methods
Keywords
Characteristic Peaks Of Infrared Spectrum, Second Derivative, Articular Cartilage, Collagen, Proteoglycan
Abstract
As a novel and efficient spectroscopic technology, Fourier transform infrared spectroscopic imaging (FTIR) can obtain information on the composition and structure of samples at high resolution, and has begun to be deeply applied in the field of biomedical photonics research. This article uses ftiri technology to study the infrared spectrum imaging and analysis methods of the main components of articular cartilage (collagen and proteoglycan pg). First, ftir imaging and infrared spectrum analysis were performed on multiple groups of cartilage slices, and then the characteristic peak intensity integration method and the quadratic derivation method were used to characterize these characteristic bands (amidei, ii, iii and sugar) respectively, and two principal components or characteristics were given. Relationship between group content and cartilage depth. Secondly, the principal component regression method is used to quantitatively calculate the concentrations of the two principal components, and the correlation between these concentrations and the integrated area of the spectral characteristic peak at the corresponding position and the peak area after the second derivation are studied. The results show that the integrated intensity of the characteristic peaks of amidi and amidii has the highest correlation with collagen concentration. After the second derivation, the sugar band intensity has the highest correlation with the proteoglycan concentration. These results indicate that the integrated intensity of the amidi and amideii bands is suitable for qualitatively expressing the content of collagen and its change with depth, while the quadratic derivation intensity of the sugar band is more suitable for qualitatively expressing the content of proteoglycan and its change with depth. . Amidiii band integration and quadratic derivation are neither suitable for characterizing collagen nor pg content. This study provides a faster and more practical method for early research on articular cartilage and osteoarthritis, thereby facilitating the judgment and repair monitoring of early osteoarthritis.
For further information of this article and research, feel free to contact our team for asssitance.
Original research was done by Wu Yuechao, Yin Jianhua, Liu Yu,
About ETChem
ETChem, a reputable Chinese Collagen factory manufacturer and supplier, is renowned for producing, stocking, exporting, and delivering the highest quality collagens. They include marine collagen, fish collagen, bovine collagen, chicken collagen, type I collagen, type II collagen and type III collagen etc. Their offerings, characterized by a neutral taste, and instant solubility attributes, cater to a diverse range of industries. They serve nutraceutical, pharmaceutical, cosmeceutical, veterinary, as well as food and beverage finished product distributors, traders, and manufacturers across Europe, USA, Canada, Australia, Thailand, Japan, Korea, Brazil, and Chile, among others.
ETChem specialization includes exporting and delivering tailor-made collagen powder and finished collagen nutritional supplements. Their extensive product range covers sectors like Food and Beverage, Sports Nutrition, Weight Management, Dietary Supplements, Health and Wellness Products, ensuring comprehensive solutions to meet all your protein needs.
As a trusted company by leading global food and beverage brands and Fortune 500 companies, ETChem reinforces China’s reputation in the global arena. For more information or to sample their products, please contact them and email karen(at)et-chem.com today.
