从内到外诱导β-肽结构

日本的研究人员发现,β-肽链的氟化会影响它们的稳定性。安西娅·布莱克本写的更多…

定做的合成肽链represents a powerful tool for tuning the structure and properties of peptides,考虑到开发医学类似物,技术和合成目的。

例如,theβ-肽is a synthetic peptide,哪一个,in contrast to its naturally-occurring α-peptide analogue,is bonded through the β-carbon rather than the α-carbon.由于这种看似微小的结构变化,观察到肽的二级结构和热力学稳定性的变化。

在肽链中加入氟化物基团代表了另一种方法,通过存在更强的氢键和引入无氟性来改变和稳定折叠结构。This approach is generally employed for the addition of fluoride groups at ‘remote positions,' spaced two or more methylene units from the peptide backbone.However,这种方法对肽本身的构象影响较小,而主要影响肽链的三级和四级自聚集,as a result of the fluorophilic effect of the functionalised peptide chains.

更不常见的研究是在肽链的“直接接近”中加入氟基的影响,也就是说,直接附着在β-碳上,如果建议直接影响分子内氢键,因此,肽链的二级结构也是如此。

石田and co-workers from the里肯紧急物质科学中心新利手机客户端已经证明β-肽的“直接”氟化可以,事实上,影响这些肽链的高阶结构。明确地,设计了一种六聚体β-肽,包括1位、3位、4位和6位的环己烷基β-氨基酸和2位和5位的L-丙氨酸衍生物,where the L-alanine methyl groups were either native or perfluorinated.

不管β肽的全氟化程度如何,结果发现,这些链是以同样的左手14螺旋结构排列的。with the NH-amide of the second and fifth residues participating in stabilising intramolecular H-bonding interactions.Moreover,it was found that although the presence of fluoride groups did not noticeably alter the overall secondary structure of the β-peptide chains,这些结构的稳定性显著提高,表明氟化物基团对NH酰胺的氢键给药能力有显著影响。

This new approach of modifying peptide chains offers an interesting method  for influencing the secondary,and higher order,化合物的结构,as well as their kinetic and thermodynamic properties.这些结构修饰的影响提供了调整这些肽链的化学和生物学特性的可能性,以用于新型抗生素和合成系统。

读这个热点化学通讯article in full!

Stabilization ofβ-peptide helices by direct attachment of trifluoromethyl groups to peptide backbones
Joonil ChoKyohei SawakiShinya Hanashima,山口吉,Motoo Shiro,Kazuhiko Saigo和Yasuhiro Ishida
化学。共同体。二千零一十四50,9855–9858.

About the Writer

安西娅·布莱克本是化学通讯的客座网络作家。Antheais a graduate student hailing from New Zealand,studying at Northwestern University in the US under the tutelage of教授弗雷泽·斯托达特(Scot)在那里,她利用超分子化学来发展多维系统,并研究这些超结构中出现的新兴性质。新利手机客户端When time and money allow,她雄心勃勃地试图在毕业前访问美国50个州。

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