Protamine‐induced condensation of peptide nanofilaments into twisted bundles with controlled helical geometry. (15th July 2019)

• Record Type: Journal Article
• Authors: Wang, Jiahui; Jia, Jiajia; Wang, Yuefei; Xing, Qiguo; Peng, Xin; Qi, Wei; Su, Rongxin; He, Zhimin
• Is Part Of: Journal of peptide science. Volume 25:Number 7(2019)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2019-07-15
• Subjects: peptide -- protamine -- coassembly -- helical structure -- macromolecular crowding; Peptides -- Periodicals; Peptides -- Periodicals; 572.65
• DOI: 10.1002/psc.3176
• Languages: English
• ISSNs: 1075-2617

Abstract

Abstract : Chiral self‐assembly of peptides is of fundamental interest in the field of biology and material science. Protamine, an alkaline biomacromolecule which is ubiquitous in fish and mammalian, plays crucial roles in directing the helical twisting of DNA. Inspired by this, we reported a bioinspired pathway to direct the hierarchical chiral self‐assembly of a short synthetic dipeptide. The peptide could self‐assemble into negatively charged chiral micelles in water that spontaneously formed a nematic liquid crystalline phase. By incorporation with protamine, the micelles condensed with the protamine into large helical bundles with precisely controlled diameter. Furthermore, to simulate the intracellular environments, we investigated macromolecular crowding on the coassembly of peptide and protamine, which leads to the formation of much thinner helical structures. The results highlight the roles of highly charged biomacromolecules and macromolecular crowding on peptide self‐assembly, which are beneficial for the practical applications of self‐assembling peptides in biomedicine and sensing. Abstract : A bioinspired pathway to direct peptide hierarchical chiral self‐assembly is reported. The peptide could self‐assemble into negatively charged chiral micelles in water that spontaneously formed a nematic liquid crystalline phase. By incorporation with protamine, the micelles condensed with the protamine into large helical bundles with precisely controlled diameter.