首页> 外文期刊>Scientific reports. >Ligand binding to an Allergenic Lipid Transfer Protein Enhances Conformational Flexibility resulting in an Increase in Susceptibility to Gastroduodenal Proteolysis
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Ligand binding to an Allergenic Lipid Transfer Protein Enhances Conformational Flexibility resulting in an Increase in Susceptibility to Gastroduodenal Proteolysis

机译:配体与变应性脂质转移蛋白的结合增强构象柔韧性,导致胃十二指肠蛋白水解的敏感性增加

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Non-specific lipid transfer proteins (LTPs) are a family of lipid-binding molecules that are widely distributed across flowering plant species, many of which have been identified as allergens. They are highly resistant to simulated gastroduodenal proteolysis, a property that may play a role in determining their allergenicity and it has been suggested that lipid binding may further increase stability to proteolysis. It is demonstrated that LTPs from wheat and peach bind a range of lipids in a variety of conditions, including those found in the gastroduodenal tract. Both LTPs are initially cleaved during gastroduodenal proteolysis at three major sites between residues 39-40, 56-57 and 79-80, with wheat LTP being more resistant to cleavage than its peach ortholog. The susceptibility of wheat LTP to proteolyic cleavage increases significantly upon lipid binding. This enhanced digestibility is likely to be due to the displacement of Tyr79 and surrounding residues from the internal hydrophobic cavity upon ligand binding to the solvent exposed exterior of the LTP, facilitating proteolysis. Such knowledge contributes to our understanding as to how resistance to digestion can be used in allergenicity risk assessment of novel food proteins, including GMOs.
机译:非特异性脂质转移蛋白(LTP)是一类脂质结合分子,广泛分布于开花植物中,其中许多已被鉴定为过敏原。它们对模拟的胃十二指肠蛋白水解具有很高的抵抗力,该特性可能在确定其变应原性方面发挥作用,并且已表明脂质结合可以进一步增加对蛋白水解的稳定性。事实证明,小麦和桃子中的LTP在各种条件下(包括在十二指肠道中发现的)都结合了多种脂质。两种LTP最初在胃十二指肠蛋白水解过程中在残基39-40、56-57和79-80之间的三个主要位点处被切割,其中小麦LTP比其桃直系同源物更耐切割。脂质结合后,小麦LTP对蛋白水解的敏感性显着提高。这种增强的消化率很可能是由于配体结合到LTP外部暴露的溶剂上从而使Tyr79及其周围残基从内部疏水腔中置换出来,从而促进了蛋白水解作用。这些知识有助于我们理解如何将消化抗性用于包括GMO在内的新型食品蛋白质的致敏性风险评估中。

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