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Effects of Secondary Structure on Solid-State Hydrogen-Deuterium Exchange in Model α-Helix and β-Sheet Peptides.
Molecular Pharmaceutics ( IF 4.5 ) Pub Date : 2020-07-16 , DOI: 10.1021/acs.molpharmaceut.0c00521 Rajashekar Kammari 1 , Elizabeth M Topp 1, 2
Molecular Pharmaceutics ( IF 4.5 ) Pub Date : 2020-07-16 , DOI: 10.1021/acs.molpharmaceut.0c00521 Rajashekar Kammari 1 , Elizabeth M Topp 1, 2
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The effects of peptide secondary structure on the rate and extent of deuterium incorporation in solid-state hydrogen deuterium exchange mass spectrometry (ssHDX-MS) were assessed. Unstructured poly-d,l-alanine (PDLA) peptides, an α-helical model peptide (peptide A) and a β-sheet model peptide (peptide B), were co-lyophilized with various excipients. Peptide structures were confirmed in solution using circular dichroism (CD) spectroscopy and in the solid state with Fourier transform infrared (FTIR) spectroscopy. ssHDX-MS was conducted at two relative humidities (11 and 23% RH D2O) and deuterium uptake kinetics were monitored over 10 days. The relative contributions of peptide secondary structure and matrix interactions to deuteration incorporation were evaluated by comparing the ssHDX-MS kinetic data of peptide A and peptide B with PDLA of similar molecular weight. The results demonstrate that both peptide secondary structure and interactions with the solid matrix contribute to the protection from exchange in ssHDX-MS. A quantitative data analysis and interpretation method is presented, in which the number of protected amide bonds is calculated as the difference between the maximum deuterium incorporation in solution and in solid samples.
中文翻译：
α-螺旋和β-Sheet肽的二级结构对固态氢-氘交换的影响。
在固态氢氘交换质谱法（ssHDX-MS）中，评估了肽二级结构对氘掺入速率和程度的影响。非结构化聚d，升丙氨酸（PDLA）的肽，α螺旋模型肽（肽A）和β折叠模型肽（肽B），共转冻干与各种赋形剂。肽结构在溶液中使用圆二色性（CD）光谱确认，并在固态下通过傅立叶变换红外（FTIR）光谱确认。ssHDX-MS在两个相对湿度（相对湿度11和23％RH D 2O）和氘的吸收动力学在10天内进行了监测。通过比较肽A和肽B与分子量相似的PDLA的ssHDX-MS动力学数据，评估了肽二级结构和基质相互作用对氘掺入的相对贡献。结果表明，肽的二级结构和与固体基质的相互作用都有助于保护ssHDX-MS中的交换。提出了一种定量数据分析和解释方法，其中受保护的酰胺键的数量计算为溶液和固体样品中最大氘掺入量之间的差。
更新日期：2020-09-09
中文翻译：
α-螺旋和β-Sheet肽的二级结构对固态氢-氘交换的影响。
在固态氢氘交换质谱法（ssHDX-MS）中，评估了肽二级结构对氘掺入速率和程度的影响。非结构化聚d，升丙氨酸（PDLA）的肽，α螺旋模型肽（肽A）和β折叠模型肽（肽B），共转冻干与各种赋形剂。肽结构在溶液中使用圆二色性（CD）光谱确认，并在固态下通过傅立叶变换红外（FTIR）光谱确认。ssHDX-MS在两个相对湿度（相对湿度11和23％RH D 2O）和氘的吸收动力学在10天内进行了监测。通过比较肽A和肽B与分子量相似的PDLA的ssHDX-MS动力学数据，评估了肽二级结构和基质相互作用对氘掺入的相对贡献。结果表明，肽的二级结构和与固体基质的相互作用都有助于保护ssHDX-MS中的交换。提出了一种定量数据分析和解释方法，其中受保护的酰胺键的数量计算为溶液和固体样品中最大氘掺入量之间的差。
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