ArticleNature chemistry2015
Functionalization of cobalt porphyrin-phospholipid bilayers with his-tagged ligands and antigens.
Article in Nature chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.
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Who cites it
82 citing papers in PubMed, 155 citations in OpenAlex.
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- Fluence Rate-Dependent Kinetics of Light-Triggered Liposomal Doxorubicin Assessed by Quantitative Fluorescence-Based Endoscopic Probe.International journal of molecular sciences · 2025Article
- Binding of a Co(III) Metalloporphyrin to Amines in Water: Influence of the pInorganic chemistry · 2025Article
- Fluence rate-dependent kinetics of light-triggered liposomal doxorubicin assessed by quantitative fluorescence-based endoscopic probe.Research square · 2025Article
- Fluence rate-dependent kinetics of light-triggered liposomal doxorubicin assessed by quantitative fluorescence-based endoscopic probe.bioRxiv : the preprint server for biology · 2024Article
- Animal Models, Therapeutics, and Vaccine Approaches to Emerging and Re-Emerging Flaviviruses.Viruses · 2024Review
- Drug-phospholipid conjugate nano-assembly for drug delivery.Smart medicine · 2024Review
22 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Methods to attach polypeptides to lipid bilayers are often indirect and ineffective, and can represent a substantial bottleneck in the formation of functionalized lipid-based materials. Although the polyhistidine tag (his-tag) has been transformative in its simplicity and efficacy in binding to immobilized metals, the successful application of this approach has been challenging in physiological settings. Here we show that lipid bilayers containing porphyrin-phospholipid conjugates that are chelated with cobalt, but not with other metals, can effectively capture his-tagged proteins and peptides. The binding follows a Co(II) to Co(III) transition and occurs within the sheltered hydrophobic bilayer, resulting in an essentially irreversible attachment in serum or in a million fold excess of competing imidazole. Using this approach we anchored homing peptides into the bilayer of preformed and cargo-loaded liposomes to enable tumour targeting without disrupting the bilayer integrity. As a further demonstration, a synthetic protein fragment derived from the human immunodeficiency virus was bound to immunogenic liposomes for potent antibody generation for an otherwise non-antigenic peptide.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.