TY - JOUR
T1 - Programmable Assembly of Peptide Amphiphile via Noncovalent-to-Covalent Bond Conversion
AU - Sato, Kohei
AU - Ji, Wei
AU - Palmer, Liam C.
AU - Weber, Benjamin
AU - Barz, Matthias
AU - Stupp, Samuel I.
N1 - Funding Information:
This work was primarily supported by the Center for Bio- Inspired Energy Sciences (CBES), an Energy Frontiers Research Center (EFRC) funded by the US Department of Energy, Office of Science, Office of Basic Energy Sciences, under Award No. DE-SC0000989 for the design, synthesis, and characterization of all molecules and materials. Biological experiments were supported by the National Institutes of Health (Bioengineering Research Partnership 4R01HL116577). This work made use of the EPIC facility of Northwestern University's NUANCE Center, which has received support from the Soft and Hybrid Nanotechnology Experimental (SHyNE) Resource (NSF NNCI-1542205); the MRSEC program (NSF DMR- 1121262) at the Materials Research Center; the International Institute for Nanotechnology (IIN); the Keck Foundation; and the State of Illinois, through the IIN. This work made use of the IMSERC at Northwestern University, which has received support from the SHyNE Resource; the State of Illinois; and the IIN. The U.S. Army Research Office, the U.S. Army Medical Research and Materiel Command, and Northwestern University provided funding to develop both of these facilities, and ongoing support is received from the SHyNE Resource. Dr. Wei Ji is a postdoctoral fellow of the Research Foundation Flanders (12G2715N), and received a travel grant of long stay abroad (V468915N) from the Research Foundation Flanders (FWO-Vlaanderen), and Junior Mobility Programme (JuMo) of KU Leuven (JUMO-15-0514). Benjamin Weber and Dr. Matthias Barz acknowledge support by the German Research Council (CRC 1066-1).
Publisher Copyright:
© 2017 American Chemical Society.
PY - 2017/7/5
Y1 - 2017/7/5
N2 - Controlling the number of monomers in a supramolecular polymer has been a great challenge in programmable self-assembly of organic molecules. One approach has been to make use of frustrated growth of the supramolecular assembly by tuning the balance of attractive and repulsive intermolecular forces. We report here on the use of covalent bond formation among monomers, compensating for intermolecular electrostatic repulsion, as a mechanism to control the length of a supramolecular nanofiber formed by self-assembly of peptide amphiphiles. Circular dichroism spectroscopy in combination with dynamic light scattering, size-exclusion chromatography, and transmittance electron microscope analyses revealed that hydrogen bonds between peptides were reinforced by covalent bond formation, enabling the fiber elongation. To examine these materials for their potential biomedical applications, cytotoxicity of nanofibers against C2C12 premyoblast cells was tested. We demonstrated that cell viability increased with an increase in fiber length, presumably because of the suppressed disruption of cell membranes by the fiber end-caps.
AB - Controlling the number of monomers in a supramolecular polymer has been a great challenge in programmable self-assembly of organic molecules. One approach has been to make use of frustrated growth of the supramolecular assembly by tuning the balance of attractive and repulsive intermolecular forces. We report here on the use of covalent bond formation among monomers, compensating for intermolecular electrostatic repulsion, as a mechanism to control the length of a supramolecular nanofiber formed by self-assembly of peptide amphiphiles. Circular dichroism spectroscopy in combination with dynamic light scattering, size-exclusion chromatography, and transmittance electron microscope analyses revealed that hydrogen bonds between peptides were reinforced by covalent bond formation, enabling the fiber elongation. To examine these materials for their potential biomedical applications, cytotoxicity of nanofibers against C2C12 premyoblast cells was tested. We demonstrated that cell viability increased with an increase in fiber length, presumably because of the suppressed disruption of cell membranes by the fiber end-caps.
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U2 - 10.1021/jacs.7b03878
DO - 10.1021/jacs.7b03878
M3 - Article
C2 - 28639790
AN - SCOPUS:85021918589
SN - 0002-7863
VL - 139
SP - 8995
EP - 9000
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 26
ER -