Ayman Ismail

ORCID: 0000-0002-5275-7414
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About
Contact & Profiles
Research Areas
  • Hemophilia Treatment and Research
  • Blood properties and coagulation
  • Blood Coagulation and Thrombosis Mechanisms
  • Electrospun Nanofibers in Biomedical Applications
  • Hemoglobinopathies and Related Disorders
  • Wound Healing and Treatments
  • Biochemical and Molecular Research
  • Chronic Myeloid Leukemia Treatments
  • Hemostasis and retained surgical items
  • Iron Metabolism and Disorders
  • Cancer-related gene regulation
  • Erythrocyte Function and Pathophysiology
  • Rheology and Fluid Dynamics Studies
  • Biochemical and Structural Characterization
  • Platelet Disorders and Treatments
  • Cell Adhesion Molecules Research
  • Blood transfusion and management
  • Protease and Inhibitor Mechanisms
  • Mesenchymal stem cell research
  • CAR-T cell therapy research
  • Periodontal Regeneration and Treatments
  • Blood groups and transfusion
  • Venomous Animal Envenomation and Studies
  • Trauma, Hemostasis, Coagulopathy, Resuscitation
  • Biotin and Related Studies

Sanofi (United States)
2019-2021

University of Nebraska–Lincoln
2018-2020

Biogen (United States)
2015-2016

Plasma fibrinogen (F1) and fibronectin (pFN) polymerize to form a fibrin clot that is both hemostatic provisional matrix for wound healing. About 90% of plasma F1 has homodimeric pair γ chains (γγF1), 10% heterodimeric more acidic γ' (γγ'F1). We have synthesized novel exclusively from 1:1 (molar ratio) complex γγ'F1 pFN in the presence highly active thrombin recombinant Factor XIII (rFXIIIa). In this matrix, nanofibers were decorated with nanoclusters (termed γγ'F1:pFN fibrin). contrast,...

10.1016/j.bioactmat.2020.06.015 article EN cc-by-nc-nd Bioactive Materials 2020-07-01

Mesenchymal stem cells (MSCs) have been widely studied for tissue engineering and treating diseases in laboratories, clinical trials, clinics. Fibrin matrices are often used to culture MSCs or increase the retention of at injection site. However, fibrins made with human plasma derived fibrinogen high cost risk pathogen transmission. In this article, we if fibrin recombinant fibrinogen, thrombin, factor XIII could be deliver MSCs. We systematically investigated relationships between matrix...

10.1002/jbm.a.36508 article EN publisher-specific-oa Journal of Biomedical Materials Research Part A 2018-08-27

Abstract Sickle cell disease (SCD) is associated with hemolysis, vascular inflammation, and organ damage. Affected patients experience chronic painful vaso-occlusive events requiring hospitalization. Hypoxia-induced polymerization of sickle hemoglobin S (HbS) contributes to sickling red blood cells (RBCs) pathophysiology. Dilution HbS nonsickling or increased oxygen affinity, such as fetal bound aromatic aldehydes, clinically beneficial in decreasing polymerization. We investigated a novel...

10.1182/bloodadvances.2020003670 article EN cc-by-nc-nd Blood Advances 2021-03-04

We previously reported on a novel fibrin matrix having increased viscoelastic strength derived from human plasma fibronectin (pFN) and γγ'-fibrinogen (γγ'-FI). Here we use high pressure size exclusion chromatography (HPSEC) dynamic light scattering (DLS) to observe interactions between the linearly extended conformation of γγ'-FI random coiled pFN. Distinct γγ'-FI:pFN subpopulations were fractionated where each maintained unique retention times when individually reprocessed by HPSEC. The...

10.1016/j.ab.2020.113701 article EN cc-by-nc-nd Analytical Biochemistry 2020-04-05

Abstract Plasma fibrinogen (F1) and fibronectin (pFN) polymerize to form a fibrin clot that is both hemostatic provisional matrix for wound healing. About 90% of plasma F1 has homodimeric pair γ chains (γγF1) 10% heterodimeric more acidic γ’ (γγ’F1). We have synthesized novel exclusively from 1:1 (molar ratio) complex γγ’F1 pFN in the presence highly active thrombin recombinant Factor XIII (rFXIIIa). In this matrix, nanofibers were wrapped with periodic 200-300 nm wide nanobands (termed...

10.1101/2020.05.04.077891 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2020-05-05

Current antifibrinolytic agents reduce blood loss by inhibiting plasmin active sites (e.g., aprotinin) or preventing plasminogen/tissue plasminogen activator (tPA) binding to fibrin clots ε-aminocaproic acid and tranexamic acid); however, they have adverse side effects. Here, we expressed 60-residue (NH2NAE…IEKCOOH) Kunitz domain1 (KD1) mutants of human tissue factor pathway inhibitor type-2 that inhibit as well activation. A single (KD1-L17R-KCOOH) a double mutant (KD1-Y11T/L17R- KCOOH)...

10.3390/jcm9113684 article EN Journal of Clinical Medicine 2020-11-17
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