Coiled coil peptide-functionalized surfaces for reversible molecular binding
Abstract
We studied the conformational and self-assembly properties of de novo peptides derived from the structure of the yeast transcriptional activator GCN4 in solution and on surfaces. We showed how the pH and the polarity of the solvent directed peptide conformation and assembly. The peptides self-assembled into a coiled coil structure below pH 5 whereas they disassembled above pH 7. The presence of acetonitrile in the peptide solution influenced the peptide's ability to assemble into a coiled coil structure while retaining its alpha-helix conformation. We used these properties to control the peptide packing density on gold surfaces and demonstrated that such peptide-engineered surfaces could be used for reversible molecular binding by utilising functionalised gold nanoparticles.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
Achieving the desired balance between multiple target coiled-coil states often requires several rounds of trial-and-error and a detailed understanding of the energetic factors that discriminate between alternative topologies and oligomerization states.
“While this has been accomplished in a number of cases,18−31 achieving the desired balance between multiple target coiled-coil states often requires several rounds of trial-and-error and a detailed understanding of the energetic factors that discriminate between alternative topologies and oligomerization states.”
From Assessment of the Topology and Oligomerisation States of Coiled Coils Using Metadynamics with Conformational Restraints (2025) · cites this paper as [22]
Cites
A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper Mutants
Harbury, P. B., Zhang, T., Kim, P. S., & Alber, T. (1993) · Science · doi:10.1126/science.8248779 · Cited by 1,490 · see citing works
X-Ray Structure of the GCN4 Leucine Zipper, a Two-Stranded, Parallel Coiled Coil
O’Shea, E. K., Klemm, J. D., Kim, P. S., & Alber, T. (1991) · Science · doi:10.1126/science.1948029 · Cited by 1,442 · see citing works
Designing peptide based nanomaterials
Ulijn, R. V., & Smith, A. M. (2008) · Chemical Society Reviews · doi:10.1039/b609047h · Cited by 1,139 · see citing works
Cole, M. A., Voelcker, N. H., Thissen, H. W., & Griesser, H. J. (2009) · Biomaterials · doi:10.1016/j.biomaterials.2008.12.026 · Cited by 454 · see citing works
Peptide ‘Velcro’: Design of a heterodimeric coiled coil
O’Shea, E. K., Lumb, K. J., & Kim, P. S. (1993) · Current Biology · doi:10.1016/0960-9822(93)90063-t · Cited by 437 · see citing works
Polymeric pH-sensitive membranes—A review
Zhao, C., Nie, S., Tang, M., & Sun, S. (2011) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2011.05.004 · Cited by 288 · see citing works
Apostolovic, B., Danial, M., & Klok, H. (2010) · Chemical Society Reviews · doi:10.1039/b914339b · Cited by 287 · see citing works
Doxorubicin Uptake and Release from Microgel Thin Films
Serpe, M. J., Yarmey, K. A., Nolan, C. M., & Lyon, L. A. (2004) · Biomacromolecules · doi:10.1021/bm049455x · Cited by 222 · see citing works
Predicting oligomerization states of coiled coils
Woolfson, D. N., & Alber, T. (1995) · Protein Science · doi:10.1002/pro.5560040818 · Cited by 214 · see citing works
A Periodic Table of Coiled-Coil Protein Structures
Moutevelis, E., & Woolfson, D. N. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.11.028 · Cited by 204 · see citing works
Thermally Modulated Insulin Release from Microgel Thin Films
Nolan, C. M., Serpe, M. J., & Lyon, L. A. (2004) · Biomacromolecules · doi:10.1021/bm049750h · Cited by 200 · see citing works
Coiled‐Coil Peptide‐Based Assembly of Gold Nanoparticles
Stevens, M. M., Flynn, N. T., Wang, C., Tirrell, D. A., & Langer, R. (2004) · Advanced Materials · doi:10.1002/adma.200306430 · Cited by 170 · see citing works
Hydrogel Microparticles as Dynamically Tunable Microlenses
Kim, J., Serpe, M. J., & Lyon, L. A. (2004) · Journal of the American Chemical Society · doi:10.1021/ja047274x · Cited by 161 · see citing works
Acetonitrile-protein interactions: amino acid solubility and preferential solvation
Gekko, K., Ohmae, E., Kameyama, K., & Takagi, T. (1998) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(98)00121-6 · Cited by 149 · see citing works
The design of antiparallel coiled coils
Oakley, M. G. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00232-3 · Cited by 131 · see citing works
Chang, Y., Meng, X., Zhao, Y., Li, K., Zhao, B., Zhu, M. J., Li, Y., Chen, X., & Wang, J. (2011) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2011.06.086 · Cited by 125 · see citing works
Wu, K., Liu, J., Johnson, R. N., Yang, J., & Kopec̆ek, J. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.200906232 · Cited by 120 · see citing works
Zareie, H. M., Boyer, C. A., Bulmuş, V., Nateghi, E., & Davis, T. P. (2008) · ACS Nano · doi:10.1021/nn800076h · Cited by 114 · see citing works
Mihályi, E. (1968) · Journal of Chemical & Engineering Data · doi:10.1021/je60037a011 · Cited by 111 · see citing works
Bioresponsive peptide–inorganic hybrid nanomaterials
Aili, D., & Stevens, M. M. (2010) · Chemical Society Reviews · doi:10.1039/b919461b · Cited by 109 · see citing works
Photoswitchable Microlens Arrays
Kim, J., Serpe, M. J., & Lyon, L. A. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200461538 · Cited by 98 · see citing works
Kinase‐Actuated Immunoaggregation of Peptide‐Conjugated Gold Nanoparticles
Gupta, S., Andresen, H., Ghadiali, J. E., & Stevens, M. M. (2010) · Small · doi:10.1002/smll.201000099 · Cited by 79 · see citing works
Self-citationThe retro -GCN4 leucine zipper sequence forms a stable three-dimensional structure
Mittl, P. R. E., Deillon, C., Sargent, D. F., Liu, N., Klauser, S., Thomas, R. M., Gutte, B., & Grütter, M. G. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.6.2562 · Cited by 73 · see citing works
Ag/ZnO nanomaterials as high performance sensors for flammable and toxic gases
Simon, Q., Barreca, D., Gasparotto, A., Maccato, C., Tondello, E., Sada, C., Comini, E., Devi, A., & Fischer, R. A. (2011) · Nanotechnology · doi:10.1088/0957-4484/23/2/025502 · Cited by 61 · see citing works
pH-Dependent Behavior of Surface-immobilized Artificial Leucine Zipper Proteins
Stevens, M. M., Allen, S., Sakata, J. K., Davies, M. C., Roberts, C. J., Tendler, S. J. B., Tirrell, D. A., & Williams, P. M. (2004) · Langmuir · doi:10.1021/la030440e · Cited by 48 · see citing works
Single-step kinase inhibitor screening using a peptide-modified gold nanoparticle platform
Gupta, S., Andresen, H., & Stevens, M. M. (2011) · Chemical Communications · doi:10.1039/c0cc04903d · Cited by 40 · see citing works
Self-citationWagner, S. C., Roskamp, M., Cölfen, H., Böttcher, C., Schlecht, S., & Koksch, B. (2008) · Organic & Biomolecular Chemistry · doi:10.1039/b813429d · Cited by 33 · see citing works
Microcantilever sensing arrays from biodegradable, pH-responsive hydrogels
VanBlarcom, D. S., & Peppas, N. A. (2011) · Biomedical Microdevices · doi:10.1007/s10544-011-9553-3 · Cited by 29 · see citing works
Tripet, B., Crescenzo, G. D., Grothé, S., O'Connor‐McCourt, M. D., & Hodges, R. S. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00883-5 · Cited by 28 · see citing works
Kashiwada, A., Tsuboi, M., Takamura, N., Brandenburg, E., Matsuda, K., & Koksch, B. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201003392 · Cited by 27 · see citing works
Dynamic heterodimer-functionalized surfaces for endothelial cell adhesion
Willcox, P. J., Reinhart‐King, C. A., Lahr, S. J., DeGrado, W. F., & Hammer, D. A. (2005) · Biomaterials · doi:10.1016/j.biomaterials.2004.11.060 · Cited by 23 · see citing works
Contarino, M., Sergi, M., Harrington, A. E., Lazareck, A. D., Xu, J. M., & CHAIKEN, I. M. (2006) · Journal of Molecular Recognition · doi:10.1002/jmr.783 · Cited by 21 · see citing works
Cachia, P. J., Kao, D., & Hodges, R. (2004) · Journal of Molecular Recognition · doi:10.1002/jmr.682 · Cited by 21 · see citing works
Shur, O., Wu, J., Cropek, D. M., & Banta, S. A. (2011) · Protein Science · doi:10.1002/pro.625 · Cited by 19 · see citing works
Acetonitrile-induced conformational transitions in poly-l-lysine
Arunkumar, A. I., Kumar, T. K. S., Sivaraman, T., & Yu, C. (1997) · International Journal of Biological Macromolecules · doi:10.1016/s0141-8130(97)00065-2 · Cited by 17 · see citing works
Gold nanoparticle self-assembly promoted by a non-covalent, charge-complemented coiled-coil peptide
Ernenwein, D., Ghosh, P., Rotello, V. M., & Chmielewski, J. A. (2010) · Journal of Materials Chemistry · doi:10.1039/c0jm01108h · Cited by 11 · see citing works
Directed surface attachment of nanomaterials via coiled-coil-driven self-assembly
White, S. J., Johnson, S., Szymonik, M., Wardingley, R. A., Pye, D., Davies, A. G., Wälti, C., & Stockley, P. G. (2012) · Nanotechnology · doi:10.1088/0957-4484/23/49/495304 · Cited by 7 · see citing works
On-Surface Assembly of Coiled-Coil Heterodimers
White, S. J., Morton, D. W. A., Cheah, B. C., Bronowska, A. K., Davies, A. G., Stockley, P. G., Wälti, C., & Johnson, S. (2012) · Langmuir · doi:10.1021/la3025149 · Cited by 7 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Zong, J., Cobb, S. L., & Cameron, N. R. (2017) · Biomaterials Science · doi:10.1039/c7bm00006e · Cited by 182 · see citing works
De novo design of tunable, pH-driven conformational changes
Boyken, S. E., Benhaim, M. A., Büsch, F., Jia, M., Bick, M. J., Choi, H., Klima, J. C., Chen, Z., Walkey, C., Mileant, A., et al. (2019) · Science · doi:10.1126/science.aav7897 · Cited by 157 · see citing works
SFG analysis of surface bound proteins: a route towards structure determination
Weidner, T., & Castner, D. G. (2013) · Physical Chemistry Chemical Physics · doi:10.1039/c3cp50880c · Cited by 92 · see citing works
Design of Stimuli‐Responsive Peptides and Proteins
Li, Y., Yang, G., Gerstweiler, L., Thang, S. H., & Zhao, C. (2022) · Advanced Functional Materials · doi:10.1002/adfm.202210387 · Cited by 70 · see citing works
Emerging Role of Injectable Dipeptide Hydrogels in Biomedical Applications
Kulkarni, N., Rao, P., Jadhav, G. S., Kulkarni, B., Kanakavalli, N., Kirad, S., Salunke, S., Tanpure, V., & Sahu, B. (2023) · ACS Omega · doi:10.1021/acsomega.2c05601 · Cited by 50 · see citing works
Layer-by-Layer Self-Assembly of Polymer Films and Capsules through Coiled-Coil Peptides
Gormley, A. J., Chandrawati, R., Christofferson, A. J., Loynachan, C. N., Jumeaux, C., Artzy‐Schnirman, A., Aili, D., Yarovsky, I., & Stevens, M. M. (2015) · Chemistry of Materials · doi:10.1021/acs.chemmater.5b02514 · Cited by 35 · see citing works
SwitCCh: Metal‐Site Design for Controlling the Assembly of a Coiled‐Coil Homodimer
Aupič, J., Lapenta, F., & Jerala, R. (2018) · ChemBioChem · doi:10.1002/cbic.201800578 · Cited by 24 · see citing works
Eibling, M. J., MacDermaid, C. M., Qian, Z., Lanci, C. J., Park, S., & Saven, J. G. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b04786 · Cited by 21 · see citing works
Hassan, H. A. F. M., Haider, M. A., & Fahmy, S. A. (2024) · Materials Advances · doi:10.1039/d4ma00075g · Cited by 17 · see citing works
Coiled Coil Crosslinked Alginate Hydrogels Dampen Macrophage-Driven Inflammation
Clapacs, Z., O’Neill, C. L., Shrimali, P. C., Lokhande, G. K., Files, M. A., Kim, D. D., Gaharwar, A. K., & Rudra, J. S. (2022) · Biomacromolecules · doi:10.1021/acs.biomac.1c01462 · Cited by 15 · see citing works
Tunable Conformation-Dependent Engineered Protein·Gold Nanoparticle Nanocomposites
Hume, J., Chen, R., Jacquet, R., Yang, M., & Montclare, J. K. (2015) · Biomacromolecules · doi:10.1021/acs.biomac.5b00098 · Cited by 12 · see citing works
Design of Tunable Protein Interfaces Controlled by Post-Translational Modifications.
Winter, D. L., Iranmanesh, H., Clark, D., & Glover, D. (2020) · ACS Synthetic Biology · doi:10.1021/acssynbio.0c00208 · Cited by 10 · see citing works
Dynamic Surface Layer Coiled Coil Proteins Processing Analog-to-Digital Information
Glionna, C., Kumar, V., Saux, G. L., Pramanik, B., Wagner, N., Cohen‐Luria, R., Ashkenasy, G., & Ashkenasy, N. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c06356 · Cited by 8 · see citing works
Peptide-based switchable and responsive surfaces
Zelzer, M. (2015) · Elsevier eBooks · doi:10.1016/b978-0-85709-713-2.00003-1 · Cited by 4 · see citing works
Notari, E., Wood, C. W., & Michel, J. (2025) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.4c01695 · Cited by 4 · see citing works
Zong, J., Cobb, S. L., & Cameron, N. R. (2021) · ARKIVOC · doi:10.24820/ark.5550190.p011.589 · Cited by 2 · see citing works
Zou, W., Xie, Z., & Du, C. (2023) · CrystEngComm · doi:10.1039/d2ce01709a · Cited by 2 · see citing works
Stimuli‐Responsive Nanostructured Surfaces for Biomedical Applications
Gomes, B. S., & Mendes, P. M. (2018) · doi:10.1002/9783527807369.ch6 · Cited by 1 · see citing works
Notari, E., Wood, C. W., & Michel, J. (2024) · ChemRxiv · doi:10.26434/chemrxiv-2024-t02df
Peptide-responsive nanocarriers for biomedical applications
Abdallah, K., Borghei, Y., Abbas, Z. N., & Hosseini, M. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-33641-6.00025-7
- Authors
- Minelli, C., Liew, J. X., Muthu, M., & Andresen, H.
- Affiliations
- National Physical Laboratory (GB)
- The University of Melbourne (AU)
- Imperial College London (GB)
- Corresponding author
- Minelli, Caterina
- ORCID
- Minelli, Caterina
- Venue
- Soft Matter
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2013
- Volume
- 9
- Issue
- 20
- Pages
- 5119
- ISSN
- 1744-683X (ISSN-L)
- 1744-6848
- OpenAlex
- W2006553095
- Cited by
- 20
- References
- 38
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2023: 2 · 2022: 2 · 2021: 2 · 2020: 1 · 2019: 1 · 2018: 2 · 2017: 2 · 2015: 3 · 2013: 1
- FWCI
- 0.51
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Soft Matter (publishedVersion)
- Topics
- Physical Sciences › Materials Science › Biomaterials › Supramolecular Self-Assembly in Materials
- Physical Sciences › Engineering › Biomedical Engineering › Surface Chemistry and Catalysis
- Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
- Keywords
- coiled-coil peptides, GCN4, peptide self-assembly, peptide conformation, pH-dependent self-assembly, solvent polarity, acetonitrile, gold surfaces, functionalized gold nanoparticles
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
