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扭曲的蛋白质聚集体与疾病:镰状血红蛋白纤维的稳定性

Twisted protein aggregates and disease: the stability of sickle hemoglobin fibers.

作者信息

Turner M S, Briehl R W, Ferrone F A, Josephs R

机构信息

Department of Physics, University of Warwick, Coventry CV4 7AL, United Kingdom.

出版信息

Phys Rev Lett. 2003 Mar 28;90(12):128103. doi: 10.1103/PhysRevLett.90.128103.

DOI:10.1103/PhysRevLett.90.128103
PMID:12688906
Abstract

We describe how twist could play an essential role in stabilizing 20 nm diameter sickle hemoglobin fibers. Our theory successfully reproduces the observed variation of helical pitch length with fiber diameter. With no remaining adjustable parameters it also yields a prediction for the torsional rigidity of sickle hemoglobin fibers that is in good agreement with experiment and hence retains the striking feature that such fibers can be highly mechanically anisotropic, even with a ratio of bending to torsional rigidity of about 50. We discuss how our study might be relevant to the development of treatment strategies.

摘要

我们描述了扭曲如何在稳定直径为20纳米的镰状血红蛋白纤维中发挥关键作用。我们的理论成功再现了观察到的螺旋节距长度随纤维直径的变化。在没有剩余可调参数的情况下,它还对镰状血红蛋白纤维的扭转刚度做出了预测,该预测与实验结果高度吻合,因此保留了一个显著特征,即即使弯曲与扭转刚度之比约为50,此类纤维仍可能具有高度的机械各向异性。我们讨论了我们的研究可能如何与治疗策略的发展相关。

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