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Functionalization of cobalt porphyrin-phospholipid bilayers with his-tagged ligands and antigens. | LitMetric

Functionalization of cobalt porphyrin-phospholipid bilayers with his-tagged ligands and antigens.

Nat Chem

1] Department of Biomedical Engineering, University at Buffalo, State University of New York, Buffalo, New York 14260, USA [2] Department of Chemical and Biological Engineering, University at Buffalo, State University of New York. Buffalo, New York 14260, USA.

Published: May 2015

AI Article Synopsis

  • Traditional methods for attaching polypeptides to lipid bilayers are often ineffective and hinder the development of lipid-based materials.
  • The study demonstrates that using cobalt-chelated porphyrin-phospholipid conjugates in lipid bilayers can effectively capture his-tagged proteins, achieving strong and stable binding.
  • This innovative method allows for the integration of homing peptides and viral protein fragments into liposomes, enhancing tumor targeting and inducing immune responses without compromising the bilayer's integrity.

Article 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.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4408904PMC
http://dx.doi.org/10.1038/nchem.2236DOI Listing

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