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Sci Rep. 2017 Jul 6;7(1):4786. doi: 10.1038/s41598-017-04727-0.

Precisely tuneable energy transfer system using peptoid helix-based molecular scaffold.

Author information

1
Department of Chemistry, School of Physics and Chemistry, Gwangju Institute of Science and Technology, 123 Cheomdan-gwagiro, Buk-gu, Gwangju, 61005, South Korea.
2
Department of Chemistry, Temple University, 1901 N. 13th St., Philadelphia, PA 19122, USA.
3
School of Earth Sciences and Engineering, Gwangju Institute of Science and Technology, 123 Cheomdan-gwagiro, Buk-gu, Gwangju, 61005, South Korea.
4
Department of Chemistry, Temple University, 1901 N. 13th St., Philadelphia, PA 19122, USA. voelz@temple.edu.
5
Department of Chemistry, School of Physics and Chemistry, Gwangju Institute of Science and Technology, 123 Cheomdan-gwagiro, Buk-gu, Gwangju, 61005, South Korea. ypang@gist.ac.kr.
6
Department of Chemistry, School of Physics and Chemistry, Gwangju Institute of Science and Technology, 123 Cheomdan-gwagiro, Buk-gu, Gwangju, 61005, South Korea. jseo@gist.ac.kr.

Abstract

The energy flow during natural photosynthesis is controlled by maintaining the spatial arrangement of pigments, employing helices as scaffolds. In this study, we have developed porphyrin-peptoid (pigment-helix) conjugates (PPCs) that can modulate the donor-acceptor energy transfer efficiency with exceptional precision by controlling the relative distance and orientation of the two pigments. Five donor-acceptor molecular dyads were constructed using zinc porphyrin and free base porphyrin (Zn(i + 2)-Zn(i + 6)), and highly efficient energy transfer was demonstrated with estimated efficiencies ranging from 92% to 96% measured by static fluorescence emission in CH2Cl2 and from 96.3% to 97.6% using femtosecond transient absorption measurements in toluene, depending on the relative spatial arrangement of the donor-acceptor pairs. Our results suggest that the remarkable precision and tunability exhibited by nature can be achieved by mimicking the design principles of natural photosynthetic proteins.

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