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Assessment of the denaturation of collagen protein concentrates using different techniques

机译：使用不同技术评估胶原蛋白浓缩物的变性

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摘要

The use of collagen and gelatin in the field of regenerative medicine is widely extended. However, most of the studies in this topic are focused on the scaffolds’ properties, but only a few are related to the properties of the raw material used. The raw material analysis not only consists of a study of the composition, but also of the denaturation degree that can influence the processing and properties of the structure of the scaffold. Thus, the denaturation degree analysis of different collagen proteins was performed and assessed by the comparison of four different methods: differential scanning calorimetry (DSC), Fourier transform Infrared Spectroscopy (FTIR) and circular dichroism (CD) spectra and sulfhydryls content analysis. DSC measurements put forward a glass transition between 88°C and 95°C as well as from the FTIR measurements; the characteristic peaks for proteins are evidenced. However, from the sulfur content, only a small proportion of free sulfhydryls are present with respect to their total amount. In addition, CD spectra allow to estimate the secondary structure of the protein by the analysis of the α-helix and β-strand and also quantify the denaturation degree with the ‘positive/negative ratio’ (RPN) from the CD profiles, obtaining values in the range between 25% and 100%.
机译：在再生药领域中使用胶原和明胶的使用是广泛的延伸。然而，本主题的大多数研究都集中在脚手架的性质上，但只有少数几个与所用原料的性质有关。原料分析不仅包括对组合物的研究，而且可以影响能够影响支架结构的处理和性质的变性程度。因此，通过对四种不同方法的比较进行和评估不同胶原蛋白的变性度分析：差示扫描量热法（DSC），傅里叶变换红外光谱（FTIR）和圆形二色性（CD）光谱和巯基含量分析。 DSC测量在88°C和95°C以及FTIR测量中提出了玻璃化转变;蛋白质的特征峰被证明。然而，从硫含量中，仅相对于它们的总量存在小比例的游离巯基。另外，CD光谱允许通过分析α-螺旋和β-链来估计蛋白质的二次结构，并从CD型材中量化与“正/负比”（RPN）的变性度，获得值在25％和100％之间的范围内。

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