Andre Francis Palmer

Last updated
Andre Francis Palmer
Palmer-Group-April-2023.jpg
Andre Palmer, Ph.D. with members of his lab
Born
Andre Francis Palmer

Port of Spain, Trinidad
NationalityAmerican
Trinidadian
Alma mater Howard University (B.S.)
Johns Hopkins University (Ph.D.)
AwardsFellow of the American Institute for Medical and Biological Engineering
Recipient of the National Science Foundation CAREER Award
Scientific career
Fields Chemical engineering
Biomolecular engineering
InstitutionsHoward University, University of Notre Dame, Ohio State University
Doctoral advisor Denis Wirtz (Ph.D.)
Website cbe.osu.edu/people/palmer.351

Andre Francis Palmer, Ph.D. is the Associate Dean for research in the College of Engineering and the Fenburr Ohio Eminent Scholar and Professor of Chemical and Biomolecular Engineering at Ohio State University. He is an expert on hemoglobin-based oxygen carriers and biomaterials used in transfusion medicine. [1]

Contents

Biography

Palmer was born in Port of Spain on the twin island Republic of Trinidad and Tobago. He is fluent in English and became a U.S. citizen. Palmer earned a chemical engineering degree at Howard University in Washington D.C in 1993 and his doctorate in chemical and biomolecular engineering at Johns Hopkins University in 1998. [2] [3]

After completing postdoctoral work at Johns Hopkins University in 1999, Palmer joined the Chemistry Department faculty at Howard University. In 2001, he left for the University of Notre Dame to become assistant professor of chemical and biomolecular engineering. [4] In 2006, after five years, he moved to Ohio State University to become associate professor of chemical and biomolecular engineering, and was promoted to full professor in 2012. He served as interim department chair in 2014–2015. [5] In 2015, he was named Chair of the William G. Lowrie Department of Chemical and Biomolecular Engineering and served until 2019. [6]

In March 2020, the Ohio Board of Regents named Palmer, "Ohio Eminent Scholar," a prestigious statewide endowed chair. [7] In August 2021, Palmer was appointed Associate Dean for research, charged with directing the College of Engineering's $138 million research enterprise. [8]

Awards and distinctions

As of 2022, Palmer has four active RO1's from the National Institutes of Health for bioengineering research projects. [9] He has multiple collaborations from research labs across the U.S. [10]

In 2021, Palmer received the Gaden Award from the Biotechnology & Bioengineering (journal) in recognition for a truly outstanding paper. [11] [12]

In 2015, Palmer was inducted fellow of the American Institute for Medical and Biological Engineering "for pioneering advances in engineering novel hemoglobin-based oxygen carriers for use as red blood cell substitutes in transfusion medicine." [13]

In 2012, Palmer received the Ohio State University's College of Engineering's Harrison Faculty Award for Excellence in Engineering Education.

In 2008, Palmer received the Lloyd Noel Ferguson Young Scientist award from the National Organization for the Professional Advancement of Chemists and Chemical Engineers (NOBCHE). [14]

In 2001, Palmer was a recipient of the National Science Foundation CAREER Award for "engineering artificial cells.” [15]

Research

Bridging the fields of chemical engineering, biochemistry, and biomaterials, Palmer's research focuses on the biophysical properties of hemoglobin, blood and plasma substitutes, and novel methods in protein purification, including interactions between adjacent cells [16]

Palmer currently holds several patents on his work. [17] [18] [19]

Hemoglobin-based oxygen carriers (HBOCs)

Palmer's lab identifies new ways to build HBOCs. Their design strategy focus on increasing the molecular diameter of HBOCs so they're unable to traverse across blood vessel walls into the tissue space and limit negative side-effects. Supporting Publications:

Facilitated oxygen transport

Palmer's research focuses on approaches to better improve oxygen storage and transport to cultured cells, especially cells grown in bioreactors. Supporting Publications:

Plasma substitutes

Palmer's lab demonstrated that human serum albumin (PolyHSA) is able to resuscitate animals from hemorrhagic shock, endotoxemia, sepsis, and ischemia reperfusion injury. Supporting publications:

Detoxification of Hemoglobin(Hb), Heme and Iron

Palmer's lab developed a hemopexin mimetic apohemoglobin (apoHb) that can scavenge heme, and when bound to Hp as the apoHb-Hp complex can scavenge and detoxify both heme and cell-free Hb. Supporting Publications:

Publications

Palmer has published over 150 peer-reviewed articles in Neuron,Transfusion Medicine,Public Library of Science,Annual Review Biomed Eng,Langmuir, Lab On A Chip,Shock,Experimental Hematology,Journal of Clinical Investigation,Science Reports, and Journal of Applied Physiology. [20]

Palmer's research portfolio is among the "top 2% of highly-cited scientists" [21] in the world [22]

Related Research Articles

<span class="mw-page-title-main">Blood</span> Organic fluid which transports nutrients throughout the organism

Blood is a body fluid in the circulatory system of humans and other vertebrates that delivers necessary substances such as nutrients and oxygen to the cells, and transports metabolic waste products away from those same cells. Blood in the circulatory system is also known as peripheral blood, and the blood cells it carries, peripheral blood cells.

<span class="mw-page-title-main">Hemoglobin</span> Oxygen-transport metalloprotein in red blood cells of most vertebrates

Hemoglobin, abbreviated Hb or Hgb, is the iron-containing oxygen-transport protein present in red blood cells (erythrocytes) of almost all vertebrates as well as the tissues of some invertebrate animals. Hemoglobin in blood carries oxygen from the respiratory organs to the other tissues of the body, where it releases the oxygen to enable aerobic respiration which powers the animal's metabolism. A healthy human has 12 to 20 grams of hemoglobin in every 100 mL of blood. Hemoglobin is a metalloprotein and chromoprotein.

<span class="mw-page-title-main">Hemoglobinopathy</span> Medical condition

Hemoglobinopathy is the medical term for a group of inherited blood disorders and diseases that primarily affect red blood cells. They are single-gene disorders and, in most cases, they are inherited as autosomal co-dominant traits.

<span class="mw-page-title-main">Myoglobin</span> Iron and oxygen-binding protein

Myoglobin is an iron- and oxygen-binding protein found in the cardiac and skeletal muscle tissue of vertebrates in general and in almost all mammals. Myoglobin is distantly related to hemoglobin. Compared to hemoglobin, myoglobin has a higher affinity for oxygen and does not have cooperative binding with oxygen like hemoglobin does. In humans, myoglobin is only found in the bloodstream after muscle injury.

<span class="mw-page-title-main">Hemoprotein</span> Protein containing a heme prosthetic group

A hemeprotein, or heme protein, is a protein that contains a heme prosthetic group. They are a very large class of metalloproteins. The heme group confers functionality, which can include oxygen carrying, oxygen reduction, electron transfer, and other processes. Heme is bound to the protein either covalently or noncovalently or both.

<span class="mw-page-title-main">Leghemoglobin</span> Phytoglobin

Leghemoglobin is an oxygen-carrying phytoglobin found in the nitrogen-fixing root nodules of leguminous plants. It is produced by these plants in response to the roots being colonized by nitrogen-fixing bacteria, termed rhizobia, as part of the symbiotic interaction between plant and bacterium: roots not colonized by Rhizobium do not synthesise leghemoglobin. Leghemoglobin has close chemical and structural similarities to hemoglobin, and, like hemoglobin, is red in colour. It was originally thought that the heme prosthetic group for plant leghemoglobin was provided by the bacterial symbiont within symbiotic root nodules. However, subsequent work shows that the plant host strongly expresses heme biosynthesis genes within nodules, and that activation of those genes correlates with leghemoglobin gene expression in developing nodules.

<span class="mw-page-title-main">Heme</span> Chemical coordination complex of an iron ion chelated to a porphyrin

Heme, or haem, is a precursor to hemoglobin, which is necessary to bind oxygen in the bloodstream. Heme is biosynthesized in both the bone marrow and the liver.

<span class="mw-page-title-main">Porphyrin</span> Heterocyclic organic compound with four modified pyrrole subunits

Porphyrins are a group of heterocyclic macrocycle organic compounds, composed of four modified pyrrole subunits interconnected at their α carbon atoms via methine bridges (=CH−). In vertebrates, an essential member of the porphyrin group is heme, which is a component of hemoproteins, whose functions include carrying oxygen in the bloodstream.

A blood substitute is a substance used to mimic and fulfill some functions of biological blood. It aims to provide an alternative to blood transfusion, which is transferring blood or blood-based products from one person into another. Thus far, there are no well-accepted oxygen-carrying blood substitutes, which is the typical objective of a red blood cell transfusion; however, there are widely available non-blood volume expanders for cases where only volume restoration is required. These are helping doctors and surgeons avoid the risks of disease transmission and immune suppression, address the chronic blood donor shortage, and address the concerns of Jehovah's Witnesses and others who have religious objections to receiving transfused blood.

<span class="mw-page-title-main">Binding site</span> Molecule-specific coordinate bonding area in biological systems

In biochemistry and molecular biology, a binding site is a region on a macromolecule such as a protein that binds to another molecule with specificity. The binding partner of the macromolecule is often referred to as a ligand. Ligands may include other proteins, enzyme substrates, second messengers, hormones, or allosteric modulators. The binding event is often, but not always, accompanied by a conformational change that alters the protein's function. Binding to protein binding sites is most often reversible, but can also be covalent reversible or irreversible.

<span class="mw-page-title-main">Fetal hemoglobin</span>

Fetal hemoglobin, or foetal haemoglobin is the main oxygen carrier protein in the human fetus. Hemoglobin F is found in fetal red blood cells, and is involved in transporting oxygen from the mother's bloodstream to organs and tissues in the fetus. It is produced at around 6 weeks of pregnancy and the levels remain high after birth until the baby is roughly 2–4 months old. Hemoglobin F has a different composition than adult forms of hemoglobin, allowing it to bind oxygen more strongly; this in turn enables the developing fetus to retrieve oxygen from the mother's bloodstream, which occurs through the placenta found in the mother's uterus.

<span class="mw-page-title-main">Conjugated protein</span> Protein that contains a non-peptide component

A conjugated protein is a protein that functions in interaction with other (non-polypeptide) chemical groups attached by covalent bonding or weak interactions.

<span class="mw-page-title-main">Human serum albumin</span> Albumin found in human blood

Human serum albumin is the serum albumin found in human blood. It is the most abundant protein in human blood plasma; it constitutes about half of serum protein. It is produced in the liver. It is soluble in water, and it is monomeric.

Iron-binding proteins are carrier proteins and metalloproteins that are important in iron metabolism and the immune response. Iron is required for life.

Biomolecular engineering is the application of engineering principles and practices to the purposeful manipulation of molecules of biological origin. Biomolecular engineers integrate knowledge of biological processes with the core knowledge of chemical engineering in order to focus on molecular level solutions to issues and problems in the life sciences related to the environment, agriculture, energy, industry, food production, biotechnology and medicine.

<span class="mw-page-title-main">Iron in biology</span> Use of Iron by organisms

Iron is an important biological element. It is used in both the ubiquitous Iron-sulfur proteins and in Vertebrates it is used in Hemoglobin which is essential for Blood and oxygen transport.

<span class="mw-page-title-main">Disuccinimidyl suberate</span> Chemical compound

Disuccinimidyl suberate (DSS) is a six-carbon lysine-reactive non-cleavable cross-linking agent.

Intravascular hemolysis describes hemolysis that happens mainly inside the vasculature. As a result, the contents of the red blood cell are released into the general circulation, leading to hemoglobinemia and increasing the risk of ensuing hyperbilirubinemia.

<span class="mw-page-title-main">Denis Wirtz</span> Belgian molecular biologist (born 1965)

Denis Wirtz is the vice provost for research and Theophilus Halley Smoot Professor of Engineering Science at Johns Hopkins University. He is an expert in the molecular and biophysical mechanisms of cell motility and adhesion and nuclear dynamics in health and disease.

Stuart L. Cooper is an American engineer. As a Full Professor and Chair of Ohio State University's Department of Chemical and Biomolecular Engineering, Cooper was elected to the National Academy of Engineering in 2011.

References

  1. "A Passion for Teaching and Research". Chemical and Biomolecular Engineering. Johns Hopkins University. Retrieved 2016-03-28.
  2. Palmer, Andre (1998). Dynamics and kinetics of actin networks in the presence of auxiliary proteins. Johns Hopkins Libraries (Thesis). Johns Hopkins University. Retrieved 2022-03-26.
  3. "Andre Palmer". University Communications. Ohio State University. Retrieved 2022-03-24.
  4. Rovner, Sophie. "Where Are They Now ?". Chemical & Engineering News. Chemical & Engineering News. Retrieved 2016-03-28.
  5. "A Passion for Teaching and Research". Whiting School of Engineering. Johns Hopkins University. Retrieved 2016-03-28.
  6. "Andre Palmer named CBE Department Chair". Chemical & Biomolecular Engineering. Ohio State University. 11 August 2015. Retrieved 2016-03-28.
  7. "Palmer named Ohio Eminent Scholar". College of Engineering. Ohio State University. Retrieved 2016-03-28.
  8. "Andre Palmer named COE Associate Dean for Research". College of Engineering. Ohio State University. Retrieved 2016-03-28.
  9. "Palmer Receives fourth New NIH RO1 in 2021". Chemical and biomolecular Engineering. Ohio State University. 21 December 2021. Retrieved 2022-03-23.
  10. "NIH Reporter Search Results". NIH Reporter. National Institutes of Health. Retrieved 2022-03-22.
  11. "Gaden Award, Past Recipients". Biotechnology and Bioengineering. John Wiley & Sons. Retrieved 2022-03-25.
  12. "Andre Palmer named COE Associate Dean for Research". College of Engineering. Ohio State University. 16 August 2021. Retrieved 2022-03-24.
  13. "Andre Palmer, Ph.D. to be inducted into Medical and Biological engineering elite" . Retrieved 2022-03-24.
  14. "Lloyd N Ferguson Young Scientist Award for Excellence in Research". NOBCCHE. NOBCCHE. Retrieved 2016-03-28.
  15. "Faculty Early Career Development (CAREER) Awards (FY 2001)". National Science Foundation. Retrieved 2022-03-25.
  16. Monczunski, John. "Building Better Blood". Notre Dame Magazine. University of Notre Dame. Retrieved 2022-03-24.
  17. "Novel Selected Protein Purification via tangential flow filtration". Office of Innovation and Economic Development. Ohio State University. 25 February 2021. Retrieved 2022-03-24.
  18. "Apoprotein manufacturing and methods for protein purification". Office of Innovation and Economic Development. Ohio State University. 30 June 2020. Retrieved 2022-03-23.
  19. "Therapeutic uses of the scavenging protein cocktail to treat plasma protein imbalances or depletion". Office of innovation and Economic Development. Ohio State University. 31 March 2021. Retrieved 2022-03-23.
  20. "Google Scholar". Google Scholar. Google Scholar. Retrieved 2016-03-28.
  21. Ioannidis, John (2021). "August 2021 data-update for "Updated science-wide author databases of standardized citation indicators". Elsevier BV. Elsevier BV. 3. doi:10.17632/btchxktzyw.3 . Retrieved 2016-03-28.
  22. "Dozens of Ohio State Engineering faculty among top 2% of highly-cited scientists". College of Engineering. Ohio State University. Retrieved 2016-03-28.