NDLI: Plasma Protein Corona Modulates the Vascular Wall Interaction of Drug Carriers in a Material and Donor Specific Manner

Content Provider	PubMed Central
Author	Sobczynski, Daniel J. Charoenphol, Phapanin Heslinga, Michael J. Onyskiw, Peter J. Namdee, Katawut Thompson, Alex J. Eniola-adefeso, Omolola
Editor	Pintus, Gianfranco
Copyright Year	2014
Abstract	The nanoscale plasma protein interaction with intravenously injected particulate carrier systems is known to modulate their organ distribution and clearance from the bloodstream. However, the role of this plasma protein interaction in prescribing the adhesion of carriers to the vascular wall remains relatively unknown. Here, we show that the adhesion of vascular-targeted poly(lactide-co-glycolic-acid) (PLGA) spheres to endothelial cells is significantly inhibited in human blood flow, with up to 90% reduction in adhesion observed relative to adhesion in simple buffer flow, depending on the particle size and the magnitude and pattern of blood flow. This reduced PLGA adhesion in blood flow is linked to the adsorption of certain high molecular weight plasma proteins on PLGA and is donor specific, where large reductions in particle adhesion in blood flow (>80% relative to buffer) is seen with ∼60% of unique donor bloods while others exhibit moderate to no reductions. The depletion of high molecular weight immunoglobulins from plasma is shown to successfully restore PLGA vascular wall adhesion. The observed plasma protein effect on PLGA is likely due to material characteristics since the effect is not replicated with polystyrene or silica spheres. These particles effectively adhere to the endothelium at a higher level in blood over buffer flow. Overall, understanding how distinct plasma proteins modulate the vascular wall interaction of vascular-targeted carriers of different material characteristics would allow for the design of highly functional delivery vehicles for the treatment of many serious human diseases.
Related Links	http://dx.doi.org/10.1371/journal.pone.0107408
Starting Page	107408
File Format	PDF
ISSN	19326203
e-ISSN	19326203
Journal	PLoS ONE
Issue Number	9
Volume Number	9
Language	English
Publisher	Public Library of Science
Publisher Date	2014-09-17
Access Restriction	Open
Rights Holder	Public Library of Science
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Specific localization of a plant cell wall glycine-rich protein in protoxylem cells of the vascular system

The Copper Metabolism MURR1 Domain Protein 1 (COMMD1) Modulates the Aggregation of Misfolded Protein Species in a Client-Specific Manner

Cyclic AMP-dependent Protein Kinase Signaling Modulates Pregnane x Receptor Activity in a Species-specific Manner*

Autophagy modulates dynamics of connexins at the plasma membrane in a ubiquitin-dependent manner

ICAM-1 engagement modulates sphingomyelinase and ceramide, supporting uptake of drug carriers by the vascular endothelium

Transcranial magnetic stimulation modulates the brain's intrinsic activity in a frequency-dependent manner

Survival motor neuron protein modulates neuron-specific apoptosis

Interaction between replication protein A and p53 is disrupted after UV damage in a DNA repair-dependent manner

Transcranial Direct Current Stimulation Modulates Human Color Discrimination in a Pathway-Specific Manner

Plasma Protein Corona Modulates the Vascular Wall Interaction of Drug Carriers in a Material and Donor Specific Manner

Similar Documents

Specific localization of a plant cell wall glycine-rich protein in protoxylem cells of the vascular system

The Copper Metabolism MURR1 Domain Protein 1 (COMMD1) Modulates the Aggregation of Misfolded Protein Species in a Client-Specific Manner

Cyclic AMP-dependent Protein Kinase Signaling Modulates Pregnane x Receptor Activity in a Species-specific Manner*

Autophagy modulates dynamics of connexins at the plasma membrane in a ubiquitin-dependent manner

ICAM-1 engagement modulates sphingomyelinase and ceramide, supporting uptake of drug carriers by the vascular endothelium

Transcranial magnetic stimulation modulates the brain's intrinsic activity in a frequency-dependent manner

Survival motor neuron protein modulates neuron-specific apoptosis

Interaction between replication protein A and p53 is disrupted after UV damage in a DNA repair-dependent manner

Transcranial Direct Current Stimulation Modulates Human Color Discrimination in a Pathway-Specific Manner

Plasma Protein Corona Modulates the Vascular Wall Interaction of Drug Carriers in a Material and Donor Specific Manner