Bolarinwa Olapeju, Nimmagadda Alekhya, Su Ma, Cai Jianfeng
Department of Chemistry, University of South Florida , 4202 East Fowler Avenue, Tampa, Florida 33620, United States.
Biochemistry. 2017 Jan 24;56(3):445-457. doi: 10.1021/acs.biochem.6b01132. Epub 2017 Jan 13.
The intrinsic drawbacks encountered in bioactive peptides in chemical biology and biomedical sciences have diverted research efforts to the development of sequence-specific peptidomimetics that are capable of mimicking the structure and function of peptides and proteins. Modifications in the backbone and/or the side chain of peptides have been explored to develop biomimetic molecular probes or drug leads for biologically important targets. To expand the family of oligomeric peptidomimetics to facilitate their further application, we recently developed a new class of peptidomimetics, AApeptides based on a chiral peptide nucleic acid backbone. AApeptides are resistant to proteolytic degradation and amenable to enormous chemical diversification. Moreover, they could mimic the primary structure of peptides and also fold into discrete secondary structure such as helices and turn-like structures. Furthermore, they have started to show promise in applications in material and biomedical sciences. Herein, we highlight the structural design and some function of AApeptides and present our perspective on their future development.
化学生物学和生物医学科学中生物活性肽所面临的内在缺陷，已将研究工作转向开发能够模拟肽和蛋白质结构与功能的序列特异性拟肽。人们已探索对肽的主链和/或侧链进行修饰，以开发针对生物学重要靶点的仿生分子探针或药物先导物。为了扩展寡聚拟肽家族以促进其进一步应用，我们最近基于手性肽核酸主链开发了一类新型拟肽——AA肽。AA肽对蛋白水解降解具有抗性，并且易于进行大量化学多样化修饰。此外，它们可以模拟肽的一级结构，还能折叠成离散的二级结构，如螺旋和类转角结构。此外，它们在材料和生物医学科学应用中已开始展现出前景。在此，我们重点介绍AA肽的结构设计和一些功能，并对其未来发展提出我们的观点。
