About

Honggang Cui is a professor of chemical and biomolecular engineering with a joint appointment in the Department of Materials Science and Engineering at Johns Hopkins University. He is known for his work developing supramolecular nanomaterials that could be used to target cancer and human diseases. Cui is also the director of doctoral admissions and holds affiliations with the Department of Oncology at the Johns Hopkins University School of Medicine, the Institute for NanoBioTechnology (INBT), and the Wilmer Eye Institute’s Center for Nanomedicine. His research exploits the unique physical, chemical, and biological properties of supramolecular nanostructures to achieve new functions that the underlying molecular building units often do not carry. His lab focuses on the design, characterization, development, optimization, and evaluation of supramolecular assemblies derived from therapeutic agents, imaging agents, and small molecule peptides. Major areas of his work include the molecular engineering and functional assembly of therapeutic agents for treating cancer, aging-related diseases, and wounds; the development of supramolecular imaging agents for disease diagnosis and treatment; and understanding the thermodynamic and kinetic factors affecting the association of small molecular building units into supramolecular polymers and networks. Cui has received several awards and honors, including being a Fellow of the American Institute for Medical and Biological Engineering, a National Sciences Foundation CAREER Award, a 3M Nontenured Faculty Award, a Johns Hopkins Catalyst Award, and a Johns Hopkins Discovery Award. He is a member of multiple professional societies, such as the American Institute of Chemical Engineers, American Chemical Society, American Peptide Society, Materials Research Society, Controlled Release Society, and Sigma Xi. Cui earned his bachelor’s degree from Beijing University of Chemical Technology in 1999, a master’s degree in chemical engineering from Tsinghua University in 2002, and a PhD in materials science and engineering from the University of Delaware in 2007. He completed postdoctoral work at Northwestern University before joining the faculty at Johns Hopkins in 2010.

Research topics

• Cancer research
• Immunology
• Pharmacology
• Medicine
• Chemistry
• Internal medicine
• Biology
• Biochemistry

Selected publications

• Balancing Chemical and Supramolecular Stability in OEGylated Supramolecular Polymers for Systemic Drug Delivery

  Journal of the American Chemical Society · 2025-05-16 · 7 citations

  articleSenior authorCorresponding

  The chemical conjugation of poly(ethylene glycol) (PEG) to therapeutic agents, known as PEGylation, is a well-established strategy for enhancing drug solubility, chemical stability, and pharmacokinetics. Here, we report on a class of supramolecular polymeric prodrugs by utilizing oligo(ethylene glycol) (OEG) to modify the hydrophobic anticancer drug camptothecin (CPT). These OEGylated prodrugs, despite their low molecular weight, spontaneously self-assemble into therapeutic supramolecular polymers (SPs) with a tubular morphology, featuring a dense OEG coating on the surface. By designing biodegradable linkers with varying chemical stabilities, we investigated how the release kinetics of CPT influence the in vitro and in vivo performance of these SPs. Our findings demonstrate that self-assembling prodrugs (SAPDs) with a self-immolative disulfanyl-ethyl carbonate (etcSS) linker exhibit a faster drug release rate than those with a reducible disulfanyl butyrate (buSS) linker, leading to higher potency and significantly improved antitumor efficacy. Notably, two stable tubular SPs, Tubustecan (TT) 1E and TT 7E, outperformed irinotecan─a clinically approved CPT prodrug─in a colon cancer model, achieving enhanced tumor growth inhibition and prolonged animal survival. These results highlight the potential of supramolecular OEGylation as an important strategy for engineering drug-based supramolecular polymers and underscore the critical role of chemical stability vs supramolecular stability in optimizing supramolecular prodrug design.

  PublisherDOI

• Self-Assembling Aromatic Peptide Amphiphile Fibers for Multivalent Display of Enzymatically Linked Antigenic Proteins

  ChemRxiv · 2025-05-28

  preprintOpen access

  Supramolecular fibers assembled from peptide amphiphiles are promising materials for the delivery of biopharmaceuticals. However, strategies for directly conjugating folded proteins onto these supramolecular dynamic assemblies remain limited. Herein, we demonstrate that aromatic peptide amphiphiles that integrate self-assembly motifs with enzymatic recognition sequences enable the synthesis of supramolecular fibrous materials amenable to protein conjugation in their native folded state. The designed peptide amphiphiles self-assembled into fibers through a combination of hydrophobic, aromatic and hydrogen bonding interactions in aqueous media. Using microbial transglutaminase, a recombinant enhanced green fluorescent protein (EGFP), used as a model proteinaceous antigen, was covalently coupled to the fibers via site-specific enzymatic cross-linking. This direct conjugation greatly enhanced the intracellular delivery of EGFP to murine dendritic cells in a man-ner dependent upon the peptide design. Notably, the resulting conjugates exhibited markedly increased immunogenicity compared to the protein alone, as evidenced by the elevated production of antigen-specific immunoglobulin G. These find-ings position the conjugated supramolecular fibers as a versatile platform for protein delivery and vaccine development.

  PublisherOA PDFDOI

• Connecting the dots: Contextualizing your work for drug delivery

  Journal of Controlled Release · 2025-01-04 · 1 citations

  editorial1st authorCorresponding
  PublisherDOI

• Self-Assembling Aromatic Peptide Amphiphile Fibers for Multivalent Display of Enzymatically Linked Antigenic Proteins

  ACS Applied Materials & Interfaces · 2025-07-23 · 1 citations

  articleOpen access

  Supramolecular fibers assembled from peptide amphiphiles are promising materials for the delivery of biopharmaceuticals. However, strategies for directly conjugating folded proteins onto these supramolecular dynamic assemblies remain limited. Herein, we demonstrate that aromatic peptide amphiphiles that integrate self-assembly motifs with enzymatic recognition sequences enable the synthesis of supramolecular fibrous materials amenable to protein conjugation in their native folded state. The designed peptide amphiphiles self-assembled into fibers through a combination of hydrophobic, aromatic, and hydrogen bonding interactions in aqueous media. Using microbial transglutaminase, a recombinant enhanced green fluorescent protein (EGFP), used as a model proteinaceous antigen, was covalently coupled to the fibers via site-specific enzymatic cross-linking. This direct conjugation greatly enhanced the intracellular delivery of EGFP to murine dendritic cells in a manner dependent upon the peptide design. Notably, the resulting conjugates exhibited markedly increased immunogenicity compared to the protein alone, as evidenced by the elevated production of antigen-specific immunoglobulin G. These findings position the conjugated supramolecular fibers as a versatile platform for protein delivery and vaccine development.

  PublisherDOI

• Peptide Materials

  Biomacromolecules · 2025-07-14 · 2 citations

  editorialCorresponding

  Over the past three decades, the field of peptide-based materials has been rapidly expanding and evolving, becoming a multidisciplinary area, with new developments and applications being consistently discovered. The purpose of this Peptide Materials Special Issue is to highlight research presented at the first Gordon Research Conference on Peptide Materials in January, 2023. Consequently, we invited eminent scientists with primary research interests in Peptide Materials to contribute original research articles or short reviews in this area. This thematic issue is focused on the materials aspects of peptides and their derivatives and mimics, including both fundamental research in peptide design, synthesis, assembly, micellization, gelation, and coacervation, as well as disparate technological applications, including functional materials for energy storage, catalysis, drug delivery, regenerative medicine, adhesion, protein purification, and nanotechnology. As peptides are composed of amino acids─the fundamental building blocks of proteins─they serve as a natural bridge between small-molecule supramolecular assemblies and large biomacromolecular constructs. Their ability to adopt well-defined secondary and tertiary structures, undergo hierarchical self-assembly, and exhibit tunable biochemical properties and distinct structural features highlights their importance and relevance within the broader landscape of biomacromolecular research. The peptide materials field has become a well-established, interdisciplinary area that attracts chemists, chemical engineers, material scientists, physicists, and biomedical engineers. The papers collected in this special issue demonstrate the growing recognition of peptides, polypeptides, proteins, and their derivatives and mimics as a versatile and critical class of biomacromolecules, poised to drive continued growth and innovation across diverse scientific and technological disciplines.

  PublisherDOI

• Drug-Inspired Design of Supramolecular Polymers for Enhanced Drug Loading and Sustained Therapeutic Release

  ACS Nano · 2025-06-30 · 4 citations

  articleOpen accessSenior authorCorresponding

  Supramolecular polymeric hydrogels have emerged as a dynamic, versatile platform for localized therapeutic delivery, leveraging reversible and tunable noncovalent interactions. Despite their potential, designing supramolecular polymers that combine high drug loading with sustained, controlled release remains a considerable challenge. Here, we introduce a series of drug-inspired, peptide-based monomers engineered as supramolecular hydrogelators to facilitate high-affinity coassembly with therapeutic agents. By strategically utilizing electrostatic complexation and π–π stacking interactions, these hydrogelators self-assemble into robust supramolecular polymer networks with well-defined nanostructures, achieving nearly 100% fingolimod loading efficiency and extremely high loading capacity (up to approximately 32% by mass). Our results demonstrate that these tailored supramolecular interactions not only enhance the fingolimod drug loading efficiency and capacity, but also modulate the self-assembly and dissociation process, enabling prolonged and predictable drug release both in vitro and in vivo. We believe this work advances the field of supramolecular polymers by integrating drug-inspired molecular design principles and contributes to the development of advanced drug delivery systems with broader biomedical applications.

  PublisherOA PDFDOI

• Effective communication with JCR editors in the peer review process

  Journal of Controlled Release · 2025-06-26

  editorialOpen access1st authorCorresponding

  Cui, Honggang; Beloqui, Ana; Brambilla, Davide; Caliceti, Paolo; Chen, Yunching Becky; Ensign, Laura M; Kim, Jong Oh; Lammers, Twan; Miyata, Kanjiro; Oh, Yu-Kyoung; Peer, Dan; Popat, Amirali; Schiffelers, Raymond; Shi, Yang; Sun, Xun; Vader, Pieter; Yeo, Yoon; Yin, Lichen; Youn, Yu Seok; Zhong, Zhiyuan; De Smedt, Stefaan C

  PublisherDOI

• High-affinity peptide biomaterials

  Current Opinion in Solid State and Materials Science · 2025-01-01 · 3 citations

  articleSenior authorCorresponding
  PublisherDOI

• Self-Assembling Peptides, Conjugates, and Mimics: A Versatile Platform for Materials and Beyond

  Accounts of Chemical Research · 2025-01-21 · 8 citations

  editorial1st authorCorresponding
  PublisherDOI

• Mitigating Membrane Biofouling in Protein Production with Zwitterionic Peptides

  Langmuir · 2025-01-06 · 6 citations

  articleSenior authorCorresponding

  Biofouling on polymeric membranes poses a significant challenge in protein production and separation processes. We report here on the use of zwitterionic peptides composed of alternating lysine (K) and glutamic acid (E) residues to reduce biomolecular fouling on gold substrates and polymeric membranes within a protein production-mimicking environment. Our findings demonstrate that both gold chips and polymeric membranes functionalized with longer sequence zwitterionic peptides, along with a hydrophilic linker, exhibit superior antifouling performance across various protein-rich environments. Furthermore, increasing the grafting density of these peptides on substrates enhances their antifouling properties. We believe that this work sheds light on the antifouling capabilities of zwitterionic peptides in cell culture environments, advancing our understanding and paving the way for the development of zwitterionic peptide-based antifouling materials for polymeric membranes.

  PublisherDOI

Recent grants

• NIH Grant R21CA191740

  NIH · $377k · 2017

• Collaborative Research: Well-Defined Polyelectrolyte Nanocages via Crystallized Miniemulsion Nanodroplets

  NSF · $255k · 2014–2017

• CDMR: Tuning the Mechanical Properties of Ordered Supramolecular Polymers and Their Networks

  NSF · $426k · 2015–2018

• Collaborative Research: DMREF: GOALI: High-Affinity Supramolecular Peptide Materials for Selective Capture and Recovery of Proteins

  NSF · $600k · 2021–2025

• CAREER: Self-Assembly of Anti-Cancer Drugs into Well-Defined Supramolecular Nanostructures

  NSF · $500k · 2013–2019

Frequent coauthors

• Hao Su

  Sichuan University

  81 shared

• Pengcheng Zhang

  Anhui University of Traditional Chinese Medicine

  74 shared

• Andrew G. Cheetham

  72 shared

• Feihu Wang

  Shanghai Jiao Tong University

  52 shared

• Han Wang

  Johns Hopkins University

  50 shared

• Ran Lin

  Guangzhou University of Chinese Medicine

  49 shared

• Caleb F. Anderson

  Frederick National Laboratory for Cancer Research

  48 shared

• Darrin J. Pochan

  University of Delaware

  44 shared

Education

• Ph.D., Materials Science and Engineering

  University of Delaware

  2007

• M.S., Chemical Engineering

  Tsinghua University

  2002

• B.S., Polymer

  Beijing University of Chemical Technology

  1999

Awards & honors

• Fellow of the American Institute for Medical and Biological…
• National Sciences Foundation CAREER Award
• 3M Nontenured Faculty Award
• Johns Hopkins Catalyst Award for early career faculty
• Johns Hopkins Discovery Award