Fibrinogen matrix deposited on the surface of biomaterials acts as a natural anti-adhesive coating

Сафиуллин, Р. А.; Christenson, Wayne; Owaynat, Hadil; Yermolenko, Ivan S.; Kadirov, Marsil K.; Ros, Robert; Ugarova, Tatiana P.

doi:10.1016/j.biomaterials.2015.07.007

Cited by 42 publications

(47 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It has been shown that hard, rough surfaces such as modified titanium and stainless steel have increased monocyte and leukocyte adhesion compared to surfaces with more yield and lower surface roughness, such as multilayered fibrinogen and our nanomatrix coating. 33–35 Our previous studies have demonstrated that our nanomatrix coating forms a stable, smooth, uniform surface on stents; this may be a critical factor in prevention of inflammatory cell adhesion. 25 Thus, the nanomatrix coating itself may be protective under flow against inflammatory cell adhesion, although the addition of NO increased this protection.…”

Section: Resultsmentioning

confidence: 94%

Novel Multifunctional Nanomatrix Reduces Inflammation in Dynamic Conditions in Vitro and Dilates Arteries ex Vivo

Alexander¹,

Vines²,

Hwang³

et al. 2016

ACS Appl. Mater. Interfaces

View full text Add to dashboard Cite

Inflammatory responses play a critical role in tissue-implant interactions, often limiting current implant utility. This is particularly true for cardiovascular devices. Existing stent technology does little to avoid or mitigate inflammation or to influence the vasomotion of the artery after implantation. We have developed a novel endothelium-mimicking nanomatrix composed of peptide amphiphiles that enhances endothelialization while decreasing both smooth muscle cell proliferation and platelet adhesion. Here, we evaluated whether the nanomatrix could prevent inflammatory responses under static and physiological flow conditions. We found that the nanomatrix reduced monocyte adhesion to endothelial cells and expression of monocyte inflammatory genes (TNF-α, MCP-1, IL-1β, and IL-6). Furthermore, the nitric-oxide releasing nanomatrix dramatically attenuated TNF-α-stimulated inflammatory responses as demonstrated by significantly reduced monocyte adhesion and inflammatory gene expression in both static and physiological flow conditions. These effects were abolished by addition of a nitric oxide scavenger. Finally, the nanomatrix stimulated vasodilation in intact rat mesenteric arterioles after constriction with phenylephrine, demonstrating the bioavailability and bioactivity of the nanomatrix, as well as exhibiting highly desired release kinetics. These results demonstrate the clinical potential of this nanomatrix by both preventing inflammatory responses and promoting vasodilation, critical improvements in stent and cardiovascular device technology.

show abstract

Section: Resultsmentioning

confidence: 94%

Novel Multifunctional Nanomatrix Reduces Inflammation in Dynamic Conditions in Vitro and Dilates Arteries ex Vivo

Alexander¹,

Vines²,

Hwang³

et al. 2016

ACS Appl. Mater. Interfaces

View full text Add to dashboard Cite

show abstract

“…8,[30][31][32][33] This region has also been directly correlated with adhesion events. [34][35][36] Fibrinogen aC region (221-610) is composed of a flexible aC connector (221-391) and a more structured aC domain (392-610). 4,7 During fibrin polymerization, crosslinking in the aC region has been shown to promote lateral aggregation and protofibril staggering.…”

Section: Introductionmentioning

confidence: 99%

Ranking reactive glutamines in the fibrinogen αC region that are targeted by blood coagulant factor XIII

Mouapi

Bell

Smith

et al. 2016

Blood

View full text Add to dashboard Cite

Key Points• FXIIIa exhibits a preference for Q237 in crosslinking reactions within fibrinogen aC (233-425) followed by Q328 and Q366.• None of the reactive glutamines in aC 233-425 (Q237, Q328, and Q366) are required to react first before the others can crosslink.Factor XIIIa (FXIIIa) introduces covalent g-glutamyl-«-lysyl crosslinks into the blood clot network. These crosslinks involve both the g and a chains of fibrin. The C-terminal portion of the fibrin a chain extends into the aC region (210-610). Crosslinks within this region help generate a stiffer clot, which is more resistant to fibrinolysis. Fibrinogen aC (233-425) contains a binding site for FXIIIa and three glutamines Q237, Q328, and Q366 that each participate in physiological crosslinking reactions. Although these glutamines were previously identified, their reactivities toward FXIIIa have not been ranked. Matrix-assisted laser desorption/ionization time of flight (MALDI-TOF) mass spectrometry and nuclear magnetic resonance (NMR) methods were thus used to directly characterize these three glutamines and probe for sources of FXIIIa substrate specificity. Glycine ethyl ester (GEE) and ammonium chloride served as replacements for lysine. Mass spectrometry and 2D heteronuclear single quantum coherence NMR revealed that Q237 is rapidly crosslinked first by FXIIIa followed by Q366 and Q328. Both N-GEE could be crosslinked to the three glutamines in aC (233-425) with a similar order of reactivity as observed with the MALDI-TOF mass spectrometry assay. NMR studies using the single aC mutants Q237N, Q328N, and Q366N demonstrated that no glutamine is dependent on another to react first in the series. Moreover, the remaining two glutamines of each mutant were both still reactive. Further characterization of Q237, Q328, and Q366 is important because they are located in a fibrinogen region susceptible to physiological truncations and mutation. The current results suggest that these glutamines play distinct roles in fibrin crosslinking and clot architecture. (Blood. 2016;127(18):2241-2248

show abstract

“…In particular, at low-density, fibrinogen forms a monolayer that directly attaches to the NP surface, 74 leading to high adhesion with platelets and leukocytes. While at high density, the fibrinogen molecules form an extensible multilayer matrix by self-assembly through the interaction between their αC domains, 75,76 this dramatically decrease cellular association under both static and flow conditions. 74,77 These results can suggest a new approach for synthesis and development of biomaterials, specifically in implantation in order to decrease initial thrombogenesis.…”

mentioning

confidence: 99%

Protein corona: a new approach for nanomedicine design

Nguyen¹,

Lee²

2017

IJN

534

343

View full text Add to dashboard Cite

After administration of nanoparticle (NP) into biological fluids, an NP–protein complex is formed, which represents the “true identity” of NP in our body. Hence, protein–NP interaction should be carefully investigated to predict and control the fate of NPs or drug-loaded NPs, including systemic circulation, biodistribution, and bioavailability. In this review, we mainly focus on the formation of protein corona and its potential applications in pharmaceutical sciences such as prediction modeling based on NP-adsorbed proteins, usage of active proteins for modifying NP to achieve toxicity reduction, circulation time enhancement, and targeting effect. Validated correlative models for NP biological responses mainly based on protein corona fingerprints of NPs are more highly accurate than the models solely set up from NP properties. Based on these models, effectiveness as well as the toxicity of NPs can be predicted without in vivo tests, while novel cell receptors could be identified from prominent proteins which play important key roles in the models. The ungoverned protein adsorption onto NPs may have generally negative effects such as rapid clearance from the bloodstream, hindrance of targeting capacity, and induction of toxicity. In contrast, controlling protein adsorption by modifying NPs with diverse functional proteins or tailoring appropriate NPs which favor selective endogenous peptides and proteins will bring promising therapeutic benefits in drug delivery and targeted cancer treatment.

show abstract

Fibrinogen matrix deposited on the surface of biomaterials acts as a natural anti-adhesive coating

Cited by 42 publications

References 45 publications

Novel Multifunctional Nanomatrix Reduces Inflammation in Dynamic Conditions in Vitro and Dilates Arteries ex Vivo

Novel Multifunctional Nanomatrix Reduces Inflammation in Dynamic Conditions in Vitro and Dilates Arteries ex Vivo

Ranking reactive glutamines in the fibrinogen αC region that are targeted by blood coagulant factor XIII

Protein corona: a new approach for nanomedicine design

Contact Info

Product

Resources

About