Abstract Alpacas (Vicugna pacos) produce a high-value fibre and leather that is increasingly sought after for the production of luxury goods. Although several studies have addressed the genetics and gene expression of alpaca skin, particularly those associated with colour, little is known about the structural and molecular compositions of alpaca skin. In this study, alpaca skin was analysed using small angle X-ray scattering (SAXS), analytical and physical methods. Using SAXS, the axial periodicity (65.1 nm) and intermolecular lateral packing distance (1.47 nm) of collagen in alpaca skin are determined to be similar to the previous studies on skins from other animal species. The collagen crosslinking profile in alpaca skin shows the presence of six crosslinks including pyridinoline and deoxypyridinoline and this is different from other animal skins. We hypothesised that the biosynthesis of pyridinoline and deoxypyridinoline in biological tissues is driven by a combination of several factors including amino acid sequence of collagen type I and lysyl hydroxylase activity. In this work, we showed that alpaca skin collagen crosslinks are diverse and their relative concentrations are different from other animal skins. We also detected histidinohydroxylysinonorleucine crosslink in alpaca skin which lacks histidine in its C-terminal telopeptide of type I collagen.

中文翻译：

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羊驼毛（Vicugna pacos）皮肤的化学和结构成分，重点关注胶原蛋白交联

摘要 羊驼 (Vicugna pacos) 生产一种高价值的纤维和皮革，越来越受到奢侈品生产的追捧。尽管一些研究已经解决了羊驼皮的遗传学和基因表达，特别是与颜色相关的那些，但对羊驼皮的结构和分子组成知之甚少。在这项研究中，使用小角 X 射线散射 (SAXS)、分析和物理方法对羊驼皮进行了分析。使用 SAXS，确定羊驼皮中胶原的轴向周期性 (65.1 nm) 和分子间横向堆积距离 (1.47 nm) 与之前对其他动物物种皮肤的研究相似。羊驼皮中的胶原交联曲线显示存在六种交联，包括吡啶啉和脱氧吡啶啉，这与其他动物皮不同。我们假设生物组织中吡啶啉和脱氧吡啶啉的生物合成是由多种因素共同驱动的，包括 I 型胶原蛋白的氨基酸序列和赖氨酰羟化酶活性。在这项工作中，我们表明羊驼皮胶原蛋白交联是多种多样的，它们的相对浓度与其他动物皮不同。我们还在羊驼皮中检测到组氨酸羟基赖氨酸正亮氨酸交联，羊驼皮的 I 型胶原蛋白 C 端端肽缺乏组氨酸。我们假设生物组织中吡啶啉和脱氧吡啶啉的生物合成是由多种因素共同驱动的，包括 I 型胶原蛋白的氨基酸序列和赖氨酰羟化酶活性。在这项工作中，我们表明羊驼皮胶原蛋白交联是多种多样的，它们的相对浓度与其他动物皮不同。我们还在羊驼皮中检测到组氨酸羟基赖氨酸正亮氨酸交联，羊驼皮的 I 型胶原蛋白 C 端端肽缺乏组氨酸。我们假设生物组织中吡啶啉和脱氧吡啶啉的生物合成是由多种因素共同驱动的，包括 I 型胶原蛋白的氨基酸序列和赖氨酰羟化酶活性。在这项工作中，我们表明羊驼皮胶原蛋白交联是多种多样的，它们的相对浓度与其他动物皮不同。我们还在羊驼皮中检测到组氨酸羟基赖氨酸正亮氨酸交联，羊驼皮的 I 型胶原蛋白 C 端端肽缺乏组氨酸。