Multicomponent peptide assemblies

Real-time analysis of amyloid fibril formation of α-synuclein using a fibrillation-state-specific fluorescent probe of JC-1

Lee, J., Lee, I., Choe, Y., Kang, S.-S., Kim, H. Y., Gai, W.-P., Hahn, J., & Paik, S. R. (2008) · Biochemical Journal · doi:10.1042/bj20081572 · Cited by 57

Insights into the consequences of co-polymerisation in the early stages of IAPP and Aβ peptide assembly from mass spectrometry

Young, L. M., Mahood, R. A., Saunders, J. C., Tu, L., Raleigh, D. P., Radford, S. E., & Ashcroft, A. E. (2015) · The Analyst · doi:10.1039/c5an00865d · Cited by 57

Mechanism of C-Terminal Fragments of Amyloid β-Protein as Aβ Inhibitors: Do C-Terminal Interactions Play a Key Role in Their Inhibitory Activity?

Zheng, X., Wu, C. F., Liu, D., Li, H., Bitan, G., Shea, J., & Bowers, M. T. (2015) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b08177 · Cited by 57

Calcium-Ion-Triggered Co-assembly of Peptide and Polysaccharide into a Hybrid Hydrogel for Drug Delivery

Xie, Y., Zhao, J., Huang, R., Qi, W., Wang, Y., Su, R., & He, Z. (2016) · Nanoscale Research Letters · doi:10.1186/s11671-016-1415-8 · Cited by 57

Controlled Supramolecular Oligomerization of C3‐Symmetrical Molecules in Water: The Impact of Hydrophobic Shielding

Besenius, P., van den Hout, K. P., Albers, H. M. H. G., de Greef, T. F. A., Olijve, L. L. C., Hermans, T. M., de Waal, B. F. M., Bomans, P. H. H., Sommerdijk, N. A. J. M., Portale, G., et al. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201002976 · Cited by 56

Synthetic SiRNA Delivery: Progress and Prospects

Roberts, T. C., Ezzat, K., Andaloussi, S. E., & Weinberg, M. S. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-3112-5_23 · Cited by 56

Self-assembled nanotubes from single fluorescent amino acid

Babar, D. G., & Sarkar, S. (2017) · Applied Nanoscience · doi:10.1007/s13204-017-0551-5 · Cited by 56

pH-Sensitive Polymeric Vesicles from Coassembly of Amphiphilic Cholate Grafted Poly( l -lysine) and Acid-Cleavable Polymer–Drug Conjugate

Zhu, L., Zhao, L., Qu, X., & Yang, Z. (2012) · Langmuir · doi:10.1021/la3015767 · Cited by 55

Morphological Diversity and Polymorphism of Self-Assembling Collagen Peptides Controlled by Length of Hydrophobic Domains

McGuinness, K. N., Khan, I. J., & Nanda, V. (2014) · ACS Nano · doi:10.1021/nn505369d · Cited by 54

Natural Polypeptide-Based Supramolecular Nanogels for Stable Noncovalent Encapsulation

Kim, K., Bae, B., Kang, Y. J., Nam, J., Kang, S., & Ryu, J. (2013) · Biomacromolecules · doi:10.1021/bm400846h · Cited by 54

Positive and Negative Design Leads to Compositional Control in AAB Collagen Heterotrimers

O’Leary, L. E. R., Fallas, J. A., & Hartgerink, J. D. (2011) · Journal of the American Chemical Society · doi:10.1021/ja111239r · Cited by 54

A peptide-based material platform for displaying antibodies to engage T cells

Zheng, Y., Wen, Y., George, A. M., Steinbach, A. M., Phillips, B. E., Giannoukakis, N., Gawalt, E. S., & Meng, W. S. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.08.083 · Cited by 53

Synergistic Inhibitory Effect of Peptide–Organic Coassemblies on Amyloid Aggregation

Niu, L., Liu, L., Xi, W., Han, Q., Li, Q., Yu, Y., Huang, Q., Qu, F., Xu, M., Li, Y., et al. (2016) · ACS Nano · doi:10.1021/acsnano.5b07396 · Cited by 53

Cooperative self-assembly of porphyrins with polymers possessing bioactive functions

Zhao, L., Qu, R., Li, A., Ma, R., & Shi, L. (2016) · Chemical Communications · doi:10.1039/c6cc05449h · Cited by 53

Creative Chemical Sensor Systems

Schrader, T. H. (2007) · Springer eBooks · doi:10.1007/978-3-540-71547-4 · Cited by 52

Compositional Control of Higher Order Assembly Using Synthetic Collagen Peptides

Xu, F., Li, J., Jain, V. K., Tu, R. S., Huang, Q., & Nanda, V. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2077894 · Cited by 52

Self-Assembling Peptide Epitopes as Novel Platform for Anticancer Vaccination

Rad‐Malekshahi, M., Fransen, M. F., Krawczyk, M., Mansourian, M., Bourajjaj, M., Chen, J., OSSENDORP, F. A., Hennink, W. E., Mastrobattista, E., & Amidi, M. (2017) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.6b01003 · Cited by 52

Inhibition of Amyloid Oligomerization into Different Supramolecular Architectures by Small Molecules: Mechanistic Insights and Design Rules

Brahmachari, S., Paul, A., Segal, D., & Gazit, E. (2017) · Future Medicinal Chemistry · doi:10.4155/fmc-2017-0026 · Cited by 52

Extracellular matrix formation in self-assembled minimalistic bioactive hydrogels based on aromatic peptide amphiphiles

Zhou, M., Ulijn, R. V., & Gough, J. E. (2014) · Journal of Tissue Engineering · doi:10.1177/2041731414531593 · Cited by 50

The Role of Protein Hydrophobicity in Conformation Change and Self-Assembly into Large Amyloid Fibers

Ridgley, D. M., Claunch, E. C., Lee, P. W., & Barone, J. R. (2014) · Biomacromolecules · doi:10.1021/bm401815u · Cited by 50

Assembly of Peptides Derived from β-Sheet Regions of β-Amyloid

Truex, N. L., Wang, Y., & Nowick, J. S. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b06000 · Cited by 50

Controlling network topology and mechanical properties of co‐assembling peptide hydrogels

Boothroyd, S. C., Saiani, A., & Miller, A. F. (2013) · Biopolymers · doi:10.1002/bip.22435 · Cited by 49

Short Peptides as Inhibitors of Amyloid Aggregation

Neddenriep, B., Calciano, A., Conti, D. J., Sauve, E., Paterson, M., Bruno, E., & Moffet, D. A. (2011) · The Open Biotechnology Journal · doi:10.2174/1874070701105010039 · Cited by 49

Stimuli-Responsive Codelivery of Oligonucleotides and Drugs by Self-Assembled Peptide Nanoparticles

Sigg, S. J., Postupalenko, V. Y., Duskey, J. T., Palivan, C. G., & Meier, W. P. (2016) · Biomacromolecules · doi:10.1021/acs.biomac.5b01614 · Cited by 48

D-amino acid-based peptide inhibitors as early or preventative therapy in Alzheimer disease

Kumar, J., & Sim, V. L. (2014) · Prion · doi:10.4161/pri.28220 · Cited by 47

Controllably degradable β-sheet nanofibers and gels from self-assembling depsipeptides

Tian, Y., Hudalla, G. A., Han, H., & Collier, J. H. (2013) · Biomaterials Science · doi:10.1039/c3bm60161g · Cited by 46

Structural Role of Counterions Adsorbed on Self-Assembled Peptide Nanotubes

Gobeaux, F., Fay, N., Tarabout, C., Mériadec, C., Meneau, F., Ligeti, M., Buisson, D., Cintrat, J., Nguyen, K. M. H., Perrin, L., et al. (2011) · Journal of the American Chemical Society · doi:10.1021/ja210299g · Cited by 46

Rational Design of Single-Composition ABC Collagen Heterotrimers

Fallas, J. A., Lee, M. A., Jalan, A. A., & Hartgerink, J. D. (2011) · Journal of the American Chemical Society · doi:10.1021/ja209669u · Cited by 46

Controlled Sub-Nanometer Epitope Spacing in a Three-Dimensional Self-Assembled Peptide Hydrogel

Pashuck, E. T., Benoit, D., Hansel, C. S., Maynard, S. A., Chow, L. W., & Stevens, M. M. (2016) · ACS Nano · doi:10.1021/acsnano.6b05975 · Cited by 46

Specification of Physiologic and Disease States by Distinct Proteins and Protein Conformations

Jarosz, D. F., & Khurana, V. (2017) · Cell · doi:10.1016/j.cell.2017.10.047 · Cited by 46

Pickering Stabilized Peptide Gel Particles as Tunable Microenvironments for Biocatalysis

Scott, G. G., Roy, S., Abul‐Haija, Y. M., Fleming, S., Bai, S., & Ulijn, R. V. (2013) · Langmuir · doi:10.1021/la403448s · Cited by 45

d-Polyglutamine Amyloid Recruits l-Polyglutamine Monomers and Kills Cells

Kar, K., Arduini, I., Drombosky, K. W., van der Wel, P. C. A., & Wetzel, R. B. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.11.019 · Cited by 45

Halogenated DOPA in a Marine Adhesive Protein

Sun, C., Srivastava, A., Reifert, J. R., & Waite, J. H. (2009) · The Journal of Adhesion · doi:10.1080/00218460902782188 · Cited by 45

C-Terminal Fragment, Aβ32–37, Analogues Protect Against Aβ Aggregation-Induced Toxicity

Bansal, S., Maurya, I. K., Yadav, N., Thota, C. K., Kumar, V., Tikoo, K., Chauhan, V. S., & Jain, R. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00006 · Cited by 45

Injectable peptide-based hydrogel formulations for the extended in vivo release of opioids

Martin, C., Oyen, E., Wanseele, Y. V., Haddou, T. B., Schmidhammer, H., Andrade, J., Waddington, L. J., Eeckhaut, A. V., Mele, B. V., Gardiner, J., et al. (2017) · Materials Today Chemistry · doi:10.1016/j.mtchem.2017.01.003 · Cited by 45

Modulating Supramolecular Peptide Hydrogel Viscoelasticity Using Biomolecular Recognition

DiMaio, J. T. M., Doran, T. M., Ryan, D. M., Raymond, D. M., & Nilsson, B. L. (2017) · Biomacromolecules · doi:10.1021/acs.biomac.7b00925 · Cited by 45

Simple Formation of an Abiotic Porphyrinogen in Aqueous Solution

Lindsey, J. S., Ptaszek, M., & Taniguchi, M. (2009) · Origins of Life and Evolution of Biospheres · doi:10.1007/s11084-009-9168-3 · Cited by 44

Tuneable pH-regulated supramolecular copolymerisation by mixing mismatched dendritic peptide comonomers

Ahlers, P., Frisch, H., & Besenius, P. (2015) · Polymer Chemistry · doi:10.1039/c5py01241d · Cited by 44

Pathological mechanisms in Huntington's disease and other polyglutamine expansion diseases

Lunkes, A., Trottier, Y., & Mandel, J. (1998) · Essays in Biochemistry · doi:10.1042/bse0330149 · Cited by 44

Phase Separation as a Possible Means of Nuclear Compartmentalization

Aumiller, W. M., Davis, B., & Keating, C. D. (2014) · International review of cytology · doi:10.1016/b978-0-12-800046-5.00005-9 · Cited by 44

Dynamic Peptide Library for the Discovery of Charge Transfer Hydrogels

Berdugo, C., Nalluri, S. K. M., Javid, N., Escuder, B., Miravet, J. F., & Ulijn, R. V. (2015) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5b08968 · Cited by 44

Supramolecular Copolymerization of Short Peptides and Polyoxometalates: toward the Fabrication of Underwater Adhesives

Xu, J., Li, X., Li, X., Li, B., Wu, L., Li, W., Xie, X., & Xue, R. (2017) · Biomacromolecules · doi:10.1021/acs.biomac.7b00817 · Cited by 44

Cross-β-Sheet Structure in Amyloid Fiber Formation

Xu, S. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp903106x · Cited by 43

Transthyretin-Derived Peptides as β-Amyloid Inhibitors

Cho, P. Y., Gururaj Joshi, A., Johnson, J. A., & Murphy, R. M. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500014u · Cited by 43

Effect of functionalization on the self-assembling propensity of β-sheet forming peptides

Taraballi, F., Campione, M., Sassella, A., Vescovi, A. L., Paleari, A., Hwang, W., & Gelain, F. (2008) · Soft Matter · doi:10.1039/b809236b · Cited by 43

3-Helix Micelles Stabilized by Polymer Springs

Dong, H., Shu, J. Y., Dube, N., Ma, Y., Tirrell, M., Downing, K. H., & Xu, T. (2012) · Journal of the American Chemical Society · doi:10.1021/ja3048128 · Cited by 43

Tuning the Inter‐nanofibril Interaction To Regulate the Morphology and Function of Peptide/DNA Co‐assembled Viral Mimics

Ni, R., & Chau, Y. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201703596 · Cited by 43

Inhibition of β-Amyloid Aggregation through a Designed β-Hairpin Peptide

Jha, A., Kumar, M. G., Gopi, H. N., & Paknikar, K. M. (2017) · Langmuir · doi:10.1021/acs.langmuir.7b03617 · Cited by 43

Coassembling Peptide-Based Biomaterials: Effects of Pairing Equal and Unequal Chain Length Oligopeptides

Ramachandran, S., Trewhella, J., Tseng, Y., & Yu, Y. B. (2006) · Chemistry of Materials · doi:10.1021/cm061071l · Cited by 42

Dissecting Electrostatic Contributions to Folding and Self-Assembly Using Designed Multicomponent Peptide Systems

Parmar, A. S., James, J. K., Grisham, D. R., Pike, D. H., & Nanda, V. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.5b10304 · Cited by 42

Optimal Interstrand Bridges for Collagen-like Biomaterials

Tanrikulu, I. C., & Raines, R. T. (2014) · Journal of the American Chemical Society · doi:10.1021/ja505426g · Cited by 42

Modulation of Amyloid β-Protein (Aβ) Assembly by Homologous C-Terminal Fragments as a Strategy for Inhibiting Aβ Toxicity

Li, H., Rahimi, F., & Bitan, G. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00154 · Cited by 42

Hierarchical self-assembly of a β-amyloid peptide derivative

Qin, S., Pei, Y., Liu, X., Zhuo, R., & Zhang, X. (2012) · Journal of Materials Chemistry B · doi:10.1039/c2tb00105e · Cited by 41

De Novo Self-Assembling Collagen Heterotrimers Using Explicit Positive and Negative Design

Xu, F., Zhang, L., Koder, R. L., & Nanda, V. (2010) · Biochemistry · doi:10.1021/bi902077d · Cited by 41

End-stapled homo and hetero collagen triple helices: a click chemistry approach

Byrne, C., McEwan, P., Emsley, J., Fischer, P. M., & Chan, W. C. (2010) · Chemical Communications · doi:10.1039/c0cc04795c · Cited by 41

Injectable peptide hydrogels for controlled-release of opioids

Martin, C., Oyen, E., Mangelschots, J., Bibian, M., Haddou, T. B., Andrade, J., Gardiner, J., Mele, B. V., Madder, A., Hoogenboom, R., et al. (2016) · MedChemComm · doi:10.1039/c5md00440c · Cited by 41

Cellular Internalization of Therapeutic Oligonucleotides by Peptide Amphiphile Nanofibers and Nanospheres

Mumcuoglu, D., Ekiz, M. Ş., Gunay, G., Tekinay, T., Tekinay, A. B., & Guler, M. O. (2016) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6b01526 · Cited by 41

Wettability gradient-induced alignment of peptide nanotubes as templates for biosensing applications

Almohammed, S., Oladapo, S. O., Ryan, K., Kholkin, A. L., Rice, J. H., & Rodriguez, B. J. (2016) · RSC Advances · doi:10.1039/c6ra05732b · Cited by 41

Peptide dendrimers: drug/gene delivery and other approaches

Santos, S. D. S., Gonzaga, R. V., Silva, J. V., Savino, D. F., Prieto, D., Shikay, J. M., Silva, R. S., Paulo, L.-F., Ferreira, E. I., & Giarolla, J. (2017) · Canadian Journal of Chemistry · doi:10.1139/cjc-2017-0242 · Cited by 41

Amyloid β-peptides 1–40 and 1–42 form oligomers with mixed β-sheets

Baldassarre, M., Baronio, C. M., Morozova‐Roche, L. A., & Barth, A. (2017) · Chemical Science · doi:10.1039/c7sc01743j · Cited by 41

Triggered formation of thixotropic hydrogels by balancing competitive supramolecular synthons

Liu, K., & Steed, J. W. (2013) · Soft Matter · doi:10.1039/c3sm51949j · Cited by 40

Protein/peptide based nanomaterials for energy application

Lee, J., Lee, J. H., Lee, Y. J., & Nam, K. T. (2013) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2013.02.004 · Cited by 40

Multi-responsive polypeptide hydrogels derived from N-carboxyanhydride terpolymerizations for delivery of nonsteroidal anti-inflammatory drugs

Fan, J., Li, R., Wang, H., He, X. J., Nguyen, T. P., Letteri, R. A., Zou, J., & Wooley, K. L. (2017) · Organic & Biomolecular Chemistry · doi:10.1039/c7ob00931c · Cited by 40

Coassemblies of the Anionic Polypeptide γ-PGA and Cationic β-Sheet Peptides for Drug Delivery to Mitochondria

Cohen‐Erez, I., & Rapaport, H. (2015) · Biomacromolecules · doi:10.1021/acs.biomac.5b01140 · Cited by 39

Biocompatible, chimeric peptide-condensed supramolecular nanoparticles for tumor cell-specific siRNA delivery and gene silencing

Wang, H., Chen, W., Xie, H., Wei, X., Yin, S., Zhou, L., Xu, X., & Zheng, S. (2014) · Chemical Communications · doi:10.1039/c4cc01061b · Cited by 38

Bioengineering mini functional thymic units with EAK16-II/EAKIIH6 self-assembling hydrogel

Tajima, A., Liu, W., Pradhan, I., Bertera, S., Bagia, C., Trucco, M., Meng, W. S., & Fan, Y. (2015) · Clinical Immunology · doi:10.1016/j.clim.2015.03.010 · Cited by 37

Biomimetic Oxygen-Evolving Photobacteria Based on Amino Acid and Porphyrin Hierarchical Self-Organization

Liu, K., Zhang, H., Xing, R., Zou, Q., & Yan, X. (2017) · ACS Nano · doi:10.1021/acsnano.7b08215 · Cited by 37

Mitochondrial dysfunction induced by disease relevant AβPP and tau protein mutations

Keil, U., Hauptmann, S., Bonert, A., Scherping, I., Eckert, A., & Müller, W. E. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9206 · Cited by 36

Chirality-Mediated Mechanical and Structural Properties of Oligopeptide Hydrogels

Taraban, M. B., Feng, Y., Hammouda, B., Hyland, L. L., & Yu, Y. B. (2012) · Chemistry of Materials · doi:10.1021/cm300422q · Cited by 36

Template‐tethered collagen mimetic peptides for studying heterotrimeric triple‐helical interactions

Li, Y., Mo, X., Kim, D. J., & Yu, S. M. (2010) · Biopolymers · doi:10.1002/bip.21536 · Cited by 36

Sticky tubes and magnetic hydrogels co-assembled by a short peptide and melanin-like nanoparticles

Das, P., Yuran, S., Yan, J. W., Lee, P. S., & Reches, M. (2014) · Chemical Communications · doi:10.1039/c4cc07671k · Cited by 36

T cell epitope redundancy: cross-conservation of the TCR face between pathogens and self and its implications for vaccines and autoimmunity

Moise, L., Beseme, S., Tassone, R., Liu, R., Kibria, F., Terry, F. E., Martin, W. D., & Groot, A. S. D. (2015) · Expert Review of Vaccines · doi:10.1586/14760584.2016.1123098 · Cited by 36

Self-assembling peptides for stem cell and tissue engineering

Tatman, P. D., Muhonen, E. G., Wickers, S. T., Gee, A. O., Kim, E., & Kim, D. (2016) · Biomaterials Science · doi:10.1039/c5bm00550g · Cited by 36

Thermodynamics, morphology, and kinetics of early-stage self-assembly of π-conjugated oligopeptides

Thurston, B., Tovar, J. D., & Ferguson, A. L. (2016) · Molecular Simulation · doi:10.1080/08927022.2015.1125997 · Cited by 36

Balancing hydrophobicity and sequence pattern to influence self‐assembly of amphipathic peptides

Betush, R. J., Urban, J. M., & Nilsson, B. L. (2018) · Peptide Science · doi:10.1002/bip.23099 · Cited by 36

Functional Delivery of siRNA by Disulfide-Constrained Cyclic Amphipathic Peptides

Welch, J. J., Swanekamp, R. J., King, C., Dean, D. A., & Nilsson, B. L. (2016) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.6b00031 · Cited by 35

Co-Assembly Tags Based on Charge Complementarity (CATCH) for Installing Functional Protein Ligands into Supramolecular Biomaterials

Seroski, D. T., Restuccia, A., Sorrentino, A. D., Knox, K. R., Hagen, S. J., & Hudalla, G. A. (2016) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-016-0459-2 · Cited by 35

Oligonucleotide Delivery with Cell Surface Binding and Cell Penetrating Peptide Amphiphile Nanospheres

Mumcuoglu, D., Ekiz, M. Ş., Tekinay, T., Guler, M. O., & Tekinay, A. B. (2015) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.5b00007 · Cited by 34

Rational Design of a Non-canonical “Sticky-Ended” Collagen Triple Helix

Jalan, A. A., Jochim, K. A., & Hartgerink, J. D. (2014) · Journal of the American Chemical Society · doi:10.1021/ja5001246 · Cited by 34

Self-assembly behaviors of molecular designer functional RADA16-I peptides: influence of motifs, pH, and assembly time

Sun, Y., Zhang, Y., Tian, L., et al. (2016) · Biomedical Materials · doi:10.1088/1748-605x/12/1/015007 · Cited by 34

Molecules in medicine mini review: the αβ T cell receptor

Clambey, E. T., Davenport, B., Kappler, J. W., Marrack, P., & Homann, D. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1145-2 · Cited by 33

Alzheimer’s amyloid-β A2T variant and its N-terminal peptides inhibit amyloid-β fibrillization and rescue the induced cytotoxicity

Lin, T.-W., Chang, C., Chang, Y., Liao, Y., Yu, H., & Chen, Y. (2017) · PLoS ONE · doi:10.1371/journal.pone.0174561 · Cited by 33

Smart hydrogels from laterally-grafted peptide assembly

Li, W., Park, I., Kang, S., & Lee, M. (2012) · Chemical Communications · doi:10.1039/c2cc34528e · Cited by 32

Spontaneous Formation of a Vesicular Assembly by a Trimesic Acid Based Triple Tailed Amphiphile

Dinda, S., Ghosh, M., & Das, P. K. (2016) · Langmuir · doi:10.1021/acs.langmuir.6b01942 · Cited by 32

Peptide functionalised discotic amphiphiles and their self-assembly into supramolecular nanofibres

Besenius, P., Goedegebure, Y., Driesse, M., Koay, M. S. T., Bomans, P. H. H., Palmans, A. R. A., Dankers, P. Y. W., & Meijer, E. W. (2011) · Soft Matter · doi:10.1039/c1sm05896g · Cited by 31

Peptide Amphiphiles in Corneal Tissue Engineering

Miotto, M., Gouveia, R. M., & Connon, C. J. (2015) · Journal of Functional Biomaterials · doi:10.3390/jfb6030687 · Cited by 30

Protein–Nanoparticle Hydrogels That Self-assemble in Response to Peptide-Based Molecular Recognition

Parisi‐Amon, A., Lo, D. D., Montoro, D. T., Dewi, R. E., Longaker, M. T., & Heilshorn, S. C. (2016) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.6b00286 · Cited by 29

Small molecules that protect against β-amyloid-induced cytotoxicity by inhibiting aggregation of β-amyloid

Lee, Y. S., Kim, H. Y., Kim, Y. S., Seo, J. H., Roh, E. J., Han, H., & Shin, K. J. (2012) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2012.06.045 · Cited by 28

Design and Evaluation of Endosomolytic Biocompatible Peptides as Carriers for siRNA Delivery

Xu, W., Ran, P., Zhao, D., Chu, D., Wu, Y. F., Wang, R., Chen, B., Ding, Y., Sadatmousavi, P., Yuan, Y., et al. (2014) · Molecular Pharmaceutics · doi:10.1021/mp500429u · Cited by 28

Coassembly of Peptides Derived from β-Sheet Regions of β-Amyloid

Truex, N. L., & Nowick, J. S. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b06001 · Cited by 28

Effect of Solvent Choice on the Self‐Assembly Properties of a Diphenylalanine Amphiphile Stabilized by an Ion Pair

Mayans, E., Ballano, G., Sendros, J., Font‐Bardía, M., Campos, J. L., Puiggalı́, J., Cativiela, C., & Alemán, C. (2017) · ChemPhysChem · doi:10.1002/cphc.201700180 · Cited by 27

Fibrillar gels via the self-assembly of poly( l -glutamate)-based statistical copolymers

Vacogne, C. D., Brosnan, S. M., Mašić, A., & Schlaad, H. (2015) · Polymer Chemistry · doi:10.1039/c5py00491h · Cited by 26

Lauryl-poly-L-lysine: A New Antimicrobial Agent?

Vidal, L., Thuault, V., Mangas, A., Coveñas, R., Thienpont, A., & Geffard, M. (2014) · Journal of Amino Acids · doi:10.1155/2014/672367 · Cited by 26

Amyloid β Oligomeric Species Present in the Lag Phase of Amyloid Formation

Wolff, M., Unuchek, D., Zhang, B., Gordeliy, V., Willbold, D., & Nagel‐Steger, L. (2015) · PLoS ONE · doi:10.1371/journal.pone.0127865 · Cited by 26

Improving cartilage phenotype from differentiated pericytes in tunable peptide hydrogels

Alakpa, E. V., Jayawarna, V., Burgess, K. E., West, C. C., Péault, B., Ulijn, R. V., & Dalby, M. J. (2017) · Scientific Reports · doi:10.1038/s41598-017-07255-z · Cited by 26

Role of Intramolecular Aromatic π–π Interactions in the Self‐Assembly of Di‐ l ‐Phenylalanine Dipeptide Driven by Intermolecular Interactions: Effect of Alanine Substitution

Reddy, S. M. M., & Shanmugam, G. (2016) · ChemPhysChem · doi:10.1002/cphc.201600364 · Cited by 25

Coiled-coil helix bundle, a peptide tertiary structural motif toward hybrid functional materials

Xu, T., & Shu, J. Y. (2009) · Soft Matter · doi:10.1039/b914565f · Cited by 24

Amphiphilic Peptide–Polymer Conjugates with Side‐Conjugation

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