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Interactions of rationally designed small peptide dendrons functionalized with valine or sinapic acid with α‐helix and β‐sheet structures of poly‐l‐lysine and poly‐l‐glutamic acid
Peptide Science ( IF 2.4 ) Pub Date : 2020-03-06 , DOI: 10.1002/pep2.24155
Maja Morawiak 1 , Magdalena Stolarska 2 , Maciej Cieślak 1 , Zofia Urbanczyk‐Lipkowska 1
Affiliation  

Uncontrolled protein oligomerization leading to deposition of fibrils is related to several diseases including neurodegeneration and diabetes. Involvement of natural compounds in regulation of this process has been documented. Therefore, the design and detailed study of bioinspired new molecular entities is one of the possible avenues to achieve better therapeutics. Here, we provide experimental data derived from the application of chiraloptic methods that rationally designed, bioinspired small branched peptides influenced the primary conformation of both poly‐l‐lysine (PLL) and poly‐l‐glutamic acid (PLGA) polypeptides in a structure‐ and concentration‐dependent manner. In several cases, the circular dichroism (CD) spectra of polypeptide/dendron mixtures were considerably different from those corresponding to the individual polypeptides, in terms of significant reduction of intensity, discrete structure, and dislocation of characteristic bands. Data deconvolution suggested that compared to the individual homo‐polypeptides, the resulting polypeptide/dendron complexes had a relative gain of distorted α‐helix, and right‐ and left‐hand twisted β‐sheet forms, which may indicate a more diffuse structure. The electrostatic attraction and multiple hydrogen bonding between oppositely charged molecules, that is, between cationic‐branched peptides and the β‐sheet surface formed by anionic PLGA, might be the main cause of coaggregation that increased the variety and contribution of less ordered forms, and reduced the propensity for self‐aggregation.

中文翻译:

合理设计的缬氨酸或芥子酸官能化的小肽树突与聚赖氨酸和聚谷氨酸的α-螺旋和β-折叠结构的相互作用

导致原纤维沉积的不受控制的蛋白质低聚与多种疾病有关,包括神经退行性疾病和糖尿病。天然化合物参与该过程的调节已有文献记载。因此,生物启发的新分子实体的设计和详细研究是获得更好治疗方法的可能途径之一。在这里,我们提供了从那合理设计chiraloptic方法的应用衍生的实验数据,仿生小支链的肽既影响聚的初级构象-赖氨酸(PLL)和聚-谷氨酸(PLGA)多肽具有结构和浓度依赖性。在某些情况下,就强度,结构的离散和特征带的明显减少而言,多肽/树突混合物的圆二色性(CD)谱与对应于各个多肽的圆二色性谱有很大不同。数据反卷积表明,与单个同型多肽相比,所得多肽/树突复合物具有相对增加的扭曲的α螺旋结构以及右旋和左旋扭曲的β折叠形式,这可能表明结构更加分散。带有相反电荷的分子之间,即阳离子支链肽与阴离子PLGA形成的β-折叠表面之间的静电吸引和多个氢键,
更新日期:2020-03-06
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