121st General Meeting of the KCS

Type Poster Presentation
Area Organic Chemistry
Room No. Event Hall
Time 4월 19일 (목요일) 11:00~12:30
Code ORGN.P-528
Subject Unusual Hexagonal semi-tubular structure derived by self-assembly of terminal modified β-helical foldamer
Authors Danim Lim, Hee-Seung Lee*
Department of Chemistry, Korea Advanced Institute of Science and Technology, Korea
Abstract An area of microstructures derived from self-assembly natural as well as unnatural peptide have been shown diverse applications in various fields ranging from medicinal chemistry to nanotechnology. Particularly, self-assembled structures derived from unnatural peptide sequences – ‘foldamer’, have been exhibited intriguing physical properties which is otherwise difficult to achieve with natural sequences. Additionally, synthetic amino acid contained enhanced physical and chemical stability of oligomeric sequence. We envisioned that a simple modification at the terminus of oligomer could be an effective strategy to enhance the physical and chemical stability. In this regard, we have appended bis(benzyloxy)benzyl moiety at the C-terminus of short helical β-peptide and studied self-assembled structure and its physical properties. The peptide was prepared by coupling bis(benzyloxy)benzyl amine with the carboxylic acid part of trans-ACPC (trans-2-aminocyclopentanecarboxylic acid) hexamer building block. The morphological analysis of designed oligomer was carried out by using SEM, TEM and AFM. TEM image showed that the edge of the tube is hollow compare to the middle of the tube is filled up so that showing the unique semi-tubular structure. TGA analysis showed that this semi-microtube has thermal stability up to 300 ºC. In addition, the structure was remained stable under the acid treatment even for 15 hours. Showing the increase of both physical and chemical stability compare to the foldamer comparison. This simple terminal modification strategy of foldamer will pave the way to enhance both physical and chemical stability of self-assembled structure of peptide.
E-mail pollar79@kaist.ac.kr