Chiral Recognition of Lipid Bilayer Membranes by Supramolecular Assemblies of Peptide Amphiphiles
Open accessAbstract
On the basis of the exclusive existence of homochirality in biomolecules and the well-known phenomenon of chiral recognition, it is obvious that chirality is a crucial factor in biological events. We report here that supramolecular assemblies of peptide amphiphiles interact with lipid bilayer membranes in a stereospecific manner. When negatively charged chiral phospholipid bilayer vesicles were subjected to the assemblies, we found that peptide amphiphiles with l-amino acids show stronger affinity for the liposomes compared to the ones with d-amino acids. To examine their biological functions, we tested the cytotoxicity of nanofibers against mammalian primary cells using human bone marrow mesenchymal stem cells and murine astroglial cells. We demonstrated that cell viability increased when d-amino acids were incorporated in the structure of peptide amphiphiles, which is consistent with our finding of their weaker interactions with lipid bilayer membranes.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
There is evidence for diastereoselective permeation and enantioselective membrane binding of amino acids and peptides.
“Very few studies have probed the interactions between chiral molecules and chiral membranes, but there is evidence for diastereoselective permeation6 and enantioselective membrane binding of amino acids9 and peptides.10,11”
From Chiral lipid bilayers are enantioselectively permeable (2021) · cites this paper as [9]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Self-Assembly and Mineralization of Peptide-Amphiphile Nanofibers
Hartgerink, J. D., Beniash, E., & Stupp, S. I. (2001) · Science · doi:10.1126/science.1063187 · Cited by 3,607 · see citing works
Self-citationSelective Differentiation of Neural Progenitor Cells by High-Epitope Density Nanofibers
Silva, G. A., Czeisler, C. M., Niece, K. L., Beniash, E., Harrington, D. A., Kessler, J. A., & Stupp, S. I. (2004) · Science · doi:10.1126/science.1093783 · Cited by 2,169 · see citing works
Self-citationYashima, E., Ousaka, N., Taura, D., Shimomura, K., Ikai, T., & Maeda, K. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00354 · Cited by 2,004 · see citing works
Asymmetric Catalysis: Science and Opportunities (Nobel Lecture 2001)
Noyori, R. (2003) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.200390002 · Cited by 1,871 · see citing works
Membrane lipid composition and cellular function.
Spector, A. A., & Yorek, M. A. (1985) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)34276-0 · Cited by 1,485 · see citing works
Cell-Penetrating Peptides: From Basic Research to Clinics
Guidotti, G., Brambilla, L., & Rossi, D. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.01.003 · Cited by 1,158 · see citing works
Chirality-Sensing Supramolecular Systems
Hembury, G. A., Borovkov, V., & Inoue, Y. (2007) · Chemical Reviews · doi:10.1021/cr050005k · Cited by 1,143 · see citing works
The Distribution and Function of Phosphatidylserine in Cellular Membranes
Leventis, P. A., & Grinstein, S. (2010) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.093008.131234 · Cited by 996 · see citing works
Tysseling, V. M., Sahni, V., Niece, K. L., Birch, D. V., Czeisler, C. M., Fehlings, M. G., Stupp, S. I., & Kessler, J. A. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0143-08.2008 · Cited by 680 · see citing works
Self-citationPutting chirality to work: the strategy of chiral switches
Agranat, I., Caner, H., & Caldwell, J. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd915 · Cited by 637 · see citing works
Supramolecular Assembly of Peptide Amphiphiles
Hendricks, M. P., Sato, K., Palmer, L. C., & Stupp, S. I. (2017) · Accounts of Chemical Research · doi:10.1021/acs.accounts.7b00297 · Cited by 596 · see citing works
Self-citationEmerging chirality in nanoscience
Wang, Y., Xu, J., Wang, Y., & Chen, H. (2012) · Chemical Society Reviews · doi:10.1039/c2cs35332f · Cited by 565 · see citing works
Energy landscapes and functions of supramolecular systems
Tantakitti, F., Boekhoven, J., Wang, X., et al. (2016) · Nature Materials · doi:10.1038/nmat4538 · Cited by 467 · see citing works
Yavin, E., & Yavin, Z. (1974) · The Journal of Cell Biology · doi:10.1083/jcb.62.2.540 · Cited by 465 · see citing works
The Origin of Biological Homochirality
Blackmond, D. G. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a002147 · Cited by 408 · see citing works
Loss, Restoration, and Maintenance of Plasma Membrane Integrity
McNeil, P. L., & Steinhardt, R. A. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.137.1.1 · Cited by 339 · see citing works
Peptide supramolecular materials for therapeutics
Sato, K., Hendricks, M. P., Palmer, L. C., & Stupp, S. I. (2018) · Chemical Society Reviews · doi:10.1039/c7cs00735c · Cited by 286 · see citing works
Self-citationThe Handedness of the Universe
Hegstrom, R. A., & Kondepudi, D. K. (1990) · Scientific American · doi:10.1038/scientificamerican0190-108 · Cited by 278 · see citing works
Control of Three‐Dimensional Cell Adhesion by the Chirality of Nanofibers in Hydrogels
Liu, G., Zhang, D., & Feng, C. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201403249 · Cited by 254 · see citing works
Zhang, M., Qing, G., & Sun, T. (2011) · Chemical Society Reviews · doi:10.1039/c1cs15209b · Cited by 221 · see citing works
Fabrication of self-assembling d-form peptide nanofiber scaffold d-EAK16 for rapid hemostasis
Luo, Z., Wang, S., & Zhang, S. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.11.049 · Cited by 187 · see citing works
Gel Scaffolds of BMP‐2‐Binding Peptide Amphiphile Nanofibers for Spinal Arthrodesis
Lee, S. S., Hsu, E. L., Mendoza, M., Ghodasra, J., Nickoli, M. S., Ashtekar, A., Polavarapu, M., Babu, J., Riaz, R. M., Nicolas, J. D., et al. (2015) · Advanced Healthcare Materials · doi:10.1002/adhm.201400129 · Cited by 183 · see citing works
Self-citationInternal dynamics of a supramolecular nanofibre
Ortony, J. H., Newcomb, C. J., Matson, J. B., Palmer, L. C., Doan, P. E., Hoffman, B. M., & Stupp, S. I. (2014) · Nature Materials · doi:10.1038/nmat3979 · Cited by 171 · see citing works
Self-citationExpanding roles for diverse physical phenomena during the origin of life
Budin, I., & Szostak, J. W. (2010) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.050708.133753 · Cited by 171 · see citing works
Cell death versus cell survival instructed by supramolecular cohesion of nanostructures
Newcomb, C. J., Sur, S., Ortony, J. H., Lee, O., Matson, J. B., Boekhoven, J., Yu, J. M., Schatz, G. C., & Stupp, S. I. (2014) · Nature Communications · doi:10.1038/ncomms4321 · Cited by 165 · see citing works
Self-citationPazos, E., Sleep, E., Pérez, C. M. R., Lee, S. S., Tantakitti, F., & Stupp, S. I. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b01570 · Cited by 156 · see citing works
Self-citationda Silva, R. M. P., van der Zwaag, D., Albertazzi, L., Lee, S. S., Meijer, E. W., & Stupp, S. I. (2016) · Nature Communications · doi:10.1038/ncomms11561 · Cited by 155 · see citing works
Self-citationStereospecific Interaction between Immune Cells and Chiral Surfaces
Sun, T., Han, D. C., Rhemann, K., Chi, L., & Fuchs, H. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0686155 · Cited by 148 · see citing works
A Torsional Strain Mechanism To Tune Pitch in Supramolecular Helices
Li, L., Jiang, H., Messmore, B. W., Bull, S. R., & Stupp, S. I. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200701328 · Cited by 140 · see citing works
Self-citationEffects of surface molecular chirality on adhesion and differentiation of stem cells
Yao, X., Hu, Y., Cao, B., Peng, R., & Ding, J. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.08.013 · Cited by 138 · see citing works
Progress towards understanding β-sheet structure
Nesloney, C. L., & Kelly, J. W. (1996) · Bioorganic & Medicinal Chemistry · doi:10.1016/0968-0896(96)00051-x · Cited by 137 · see citing works
Structure, dynamics, and hydration of POPC/POPS bilayers suspended in NaCl, KCl, and CsCl solutions
Jurkiewicz, P., Cwiklik, L., Vojtíšková, A., et al. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.11.033 · Cited by 129 · see citing works
Tuning the interactions between chiral plasmonic films and living cells
Zhao, X., Xu, L., Sun, M., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-02268-8 · Cited by 126 · see citing works
Equilibrium constants for association of guanidinium and ammonium ions with oxyanions
Springs, B., & Haake, P. (1977) · Bioorganic Chemistry · doi:10.1016/0045-2068(77)90019-0 · Cited by 125 · see citing works
Presentation and Recognition of Biotin on Nanofibers Formed by Branched Peptide Amphiphiles
Guler, M. O., Soukasene, S., Hulvat, J. F., & Stupp, S. I. (2004) · Nano Letters · doi:10.1021/nl048238z · Cited by 125 · see citing works
Self-citationChiral Design for Polymeric Biointerface: The Influence of Surface Chirality on Protein Adsorption
Wang, X., Gan, H. K., & Sun, T. (2011) · Advanced Functional Materials · doi:10.1002/adfm.201101032 · Cited by 116 · see citing works
Chiral Recognition of <scp>l</scp>-Amino Acids on Liposomes Prepared with <scp>l</scp>-Phospholipid
Ishigami, T., Suga, K., & Umakoshi, H. (2015) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5b07198 · Cited by 91 · see citing works
Programmable Assembly of Peptide Amphiphile via Noncovalent-to-Covalent Bond Conversion
Sato, K., Ji, W., Palmer, L. C., et al. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b03878 · Cited by 89 · see citing works
Self-citationStereochemistry triggered differential cell behaviours on chiral polymer surfaces
Wang, X., Gan, H. K., Sun, T., Su, B., Fuchs, H., Vestweber, D., & Butz, S. (2010) · Soft Matter · doi:10.1039/c0sm00151a · Cited by 88 · see citing works
Chiral Biomaterials: From Molecular Design to Regenerative Medicine
Green, D. W., Lee, J., Kim, E., Lee, D., & Jung, H.-S. (2016) · Advanced Materials Interfaces · doi:10.1002/admi.201500411 · Cited by 79 · see citing works
Multivalent Nanofibers of a Controlled Length: Regulation of Bacterial Cell Agglutination
Lee, D.-W., Kim, T., Park, I., et al. (2012) · Journal of the American Chemical Society · doi:10.1021/ja306802m · Cited by 74 · see citing works
Modulating Cell Behaviors on Chiral Polymer Brush Films with Different Hydrophobic Side Groups
Wang, X., Gan, H. K., Zhang, M., & Sun, T. (2012) · Langmuir · doi:10.1021/la204143g · Cited by 70 · see citing works
Water Dynamics from the Surface to the Interior of a Supramolecular Nanostructure
Ortony, J. H., Qiao, B., Newcomb, C. J., Keller, T. J., Palmer, L. C., Deiss‐Yehiely, E., de la Cruz, M. O., Han, S., & Stupp, S. I. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b02969 · Cited by 70 · see citing works
Self-citationControl of Supramolecular Chirality of Nanofibers and Its Effect on Protein Adhesion
Lv, K., Zhang, L., Lü, W., & Liu, M. (2014) · ACS Applied Materials & Interfaces · doi:10.1021/am504702p · Cited by 57 · see citing works
Enhancing the Magnitude of Antibody Responses through Biomaterial Stereochemistry
Appavu, R., Chesson, C. B., Koyfman, A. Y., Snook, J. D., Kohlhapp, F. J., Zloza, A., & Rudra, J. S. (2015) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.5b00139 · Cited by 53 · see citing works
Chiral Recognition of Dipeptides in a Biomembrane Model
Bombelli, C., Borocci, S., Lupi, F., Mancini, G., Mannina, L., Segre, A. L., & Viel, S. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0470057 · Cited by 51 · see citing works
Gao, G., Zhang, M., Lu, P., Guo, G., Wang, D., & Sun, T. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201410768 · Cited by 50 · see citing works
Neuronal Growth on l - and d -Cysteine Self-Assembled Monolayers Reveals Neuronal Chiral Sensitivity
Baranes, K., Moshe, H., Alon, N., Schwartz, S., & Shefi, O. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500015s · Cited by 48 · see citing works
Chiral recognition of odorants (+)- and (-)-carvone by phospholipid monolayers
Pathirana, S., Neely, W. C., Myers, L. J., et al. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00030a041 · Cited by 48 · see citing works
Induced dye leakage by PAMAM G6 does not imply dendrimer entry into vesicle lumen
Åkesson, A., Lundgaard, C. V., Ehrlich, N., et al. (2012) · Soft Matter · doi:10.1039/c2sm25864a · Cited by 27 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- Noyori, R. Asymmetric Catalysis: Science and Opportunities (Novel Lecture). Angew. Chem., Int. Ed. 2002, 41, 2008-2022.
Cited by
Sorted by citations
Probing the Role of Chirality in Phospholipid Membranes
Martin, H. S., Podolsky, K. A., & Devaraj, N. K. (2021) · ChemBioChem · doi:10.1002/cbic.202100232 · Cited by 36 · see citing works
López, C. A., Zhang, X., Aydin, F., Shrestha, R., Van, Q. N., Stanley, C. B., Carpenter, T. S., Nguyen, K., Patel, L. A., Chen, D., et al. (2022) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.2c00168 · Cited by 18 · see citing works
- Authors
- Sato, K., Ji, W., Álvarez, Z., Palmer, L. C., & Stupp, S. I.
- Affiliations
- Northwestern University (US)
- Corresponding author
- Stupp, Samuel I.
- Venue
- ACS Biomaterials Science & Engineering
- Publisher
- American Chemical Society (ACS)
- Published
- 2019-05-29
- Volume
- 5
- Issue
- 6
- Pages
- 2786-2792
- ISSN
- 2373-9878 (ISSN-L)
- OpenAlex
- W2947557583
- Cited by
- 35
- References
- 51
- Citations by year
- 2026: 1 · 2025: 7 · 2024: 3 · 2023: 5 · 2022: 3 · 2021: 9 · 2020: 5 · 2019: 2
- FWCI
- 1.35
- Type
- journal article
- Language
- en
- Open access
- green
- www.osti.gov
- Licence
- Locations
- ACS Biomaterials Science & Engineering (publishedVersion)
- PubMed (publishedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- Fonds Wetenschappelijk Onderzoek (V468915N, 12G2718N)
- Paralyzed Veterans of America Research Foundation (PVA17_RF_0008)
- Japan Society for the Promotion of Science (18H05971)
- U.S. Department of Energy (DE-SC0000989)
- Beatriu de Pin??s - Ag??ncia de Gesti?? d'Ajust Universitaris i de Recerca (2014 BP-A 00007)
- KU Leuven Junior Mobility Programme (JUMO-15-0514)
- Topics
- Physical Sciences › Materials Science › Biomaterials › Supramolecular Self-Assembly in Materials
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
- Keywords
- chiral recognition, peptide amphiphiles, supramolecular self-assembly, lipid bilayers, L-amino acids, D-amino acids, stereospecific interactions, liposomes, nanofibers, cytotoxicity, mesenchymal stem cells, astroglial cells, homochirality
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review