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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Characterizing aggregate growth and morphology of alanine-rich polypeptides as a function of sequence chemistry and solution temperature from scattering, spectroscopy, and microscopy
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Characterizing aggregate growth and morphology of alanine-rich polypeptides as a function of sequence chemistry and solution temperature from scattering, spectroscopy, and microscopy

机译：富含丙氨酸富含多肽的聚集生长和形貌，作为散射，光谱学和显微镜的序列化学和溶液温度的函数

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摘要

The aggregation behavior and stability of a series of alanine-rich peptides, which are included as components of peptide-polymer conjugates, were characterized using a combination of biophysical techniques. Light scattering techniques were used to monitor changes in peptide morphology and size distributions as a function of time and temperature. The results show large particles immediately upon dissolution in buffer. At room temperature, these particles relaxed to reach a mostly monomeric peptide state, while at higher temperatures, they grew to form aggregates. Circular dichroism spectroscopy (CD) was used to monitor temperature- and time-dependent conformational changes as a function of peptide sequence and incubation time. CD measurements reveal that all of the sequences are helical at low temperatures with transitions to non-helical conformation with increased temperature. Samples incubated at room temperature were able to recover their original helicity. At increased temperature, the shorter and longer peptide sequences showed notable changes in conformation, and were not able to recover their original helicity after 72 h. After incubation for up to one week, beta-sheet conformations were observed in these two cases, while only alpha-helical conformation loss was observed for the peptide of intermediate molecular weight. Transmission electron microscopy measurements reveal the formation of fibrils after 72 h of incubation at 60 degrees C for all samples, in agreement with the scattering measurements. Additional quenching experiments show that peptide aggregation can be stalled when solutions are cooled to room temperature.
机译：使用生物物理技术的组合表征包括作为肽 - 聚合物缀合物组分的一系列富含丙氨酸富肽的聚集行为和稳定性。光散射技术用于监测作为时间和温度的函数的肽形态和尺寸分布的变化。结果在缓冲液中溶解时立即显示大颗粒。在室温下，这些颗粒放宽以达到最多的单体肽状态，而在较高的温度下，它们成长为聚集体。圆形二中间光谱（CD）用于监测作为肽序列和孵育时间的函数的温度和时间依赖的构象变化。 CD测量表明，所有序列都是在低温下螺旋螺旋，其与不螺旋形构象的过渡，随着温度的增加。在室温下孵育的样品能够恢复原始螺旋。在温度上升时，较短且较长较长的肽序列显示出显着的构象变化，并且在72小时后无法恢复原始螺旋状。在孵育长达一周后，在这两种情况下观察到β-薄片构象，而仅观察到中间分子量的肽的α-螺旋构象损失。透射电子显微镜测量揭示了在60摄氏度的孵育后形成原纤维的形成，以与散射测量一致。另外的淬火实验表明，当溶液冷却至室温时，可以停滞肽聚集。

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