ArticlePharmaceutical research2005
A randomly coiled, high-molecular-weight polypeptide exhibits increased paracellular diffusion in vitro and in situ relative to the highly ordered alpha-helix conformer.
Article in Pharmaceutical research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 10 citations in OpenAlex.
- Methyl-β-cyclodextrin quaternary ammonium chitosan conjugate: nanoparticles vs macromolecular soluble complex.International journal of nanomedicine · 2018Article
- Interplay of secondary structure and charge on the diffusion of a polypeptide through negatively charged aqueous pores.Pharmaceutical research · 2007Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeThe current investigation was conducted to examine the effect of secondary structure of model polypeptides on their hindered paracellular diffusion.
methodsPoly-D-glutamic acid (PDGlu) was selected as one of the model polypeptides because of its ability to form two secondary structures; a negatively charged random coil and an alpha-helix with partial negative charge at pH 7.4 and 4.7, respectively. Poly-D-lysine (PDL) was selected as a positively charged random coil conformation at pH 7.4. Transport experiments were conducted across both a Caco-2 cell monolayer and the intestinal membrane of Sprague-Dawley rats. Additionally, using NMR, an estimation for the diffusion coefficient and the equivalent hydrodynamic radius for each model polypeptide was obtained.
resultsPDGlu in the randomly coiled conformation exhibited greater paracellular transport when compared to either the same polypeptide having an alpha-helix secondary structure or the positively charged, randomly coiled PDL.
conclusionsRandomly coiled PDGlu was able to permeate through the negatively charged tight junctions of both biological membranes to a greater extent than PDGlu having an alpha-helix structure and suggests that molecular flexibility associated with the random coil conformation may play a more important role than overall charge and hydrodynamic radius on its hindered paracellular diffusion.
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Registered trials
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