Harry Chanzu Email & Phone Number

Lexington, Kentucky Area

The current project involves using knockout (KO) mouse models and human blood samples to determine the function of serglycin (SG) in platelets. SG consists of a core protein decorated by glycosaminoglycans (GAGs) chains. The project utilized (KO) mice platelets, and the team developed an assay to study the effect of SG on the packaging, sorting, and release of cargo molecules from the dense granule, 𝝰-granule, and lysosome. Using platelet factor 4 (PF4) as a marker, discovered that platelet alpha (𝝰-) granule secretion was defective in the KO animals. Dense granule and lysosomal release were comparable to the wild-type platelets. Results: Demonstrated the importance of SG in platelets 𝝰-granule release. Even if the PF4 secretion was defective in SG KO platelets, other 𝝰-granule molecules, fibrinogen, fibronectin, and vWF were unaffected. The levels of secretory machinery, SNAP-23, Syntaxin-11, VAMP-7, VAMP-8, Munc18-b, granuphilin, Rab27A, and Rab27B, and membrane proteins, P-Selectin, LAMP-1, and VMAT2 were unaffected in KO platelets. PROJECT SUMMARYDeveloped mouse colonies to study the role of SG in Platelets α-granule biogenesis, microRNA profiles in endocytosis deficient platelets, and in diseases, including cancer, inflammation, and sepsis.Involved in a federally funded research project focused on the mechanism of platelet secretion and how platelets manipulate their vascular microenvironment through the release of RNA control elements. Duties include platelet function assays, morphological studies, manuscripts, grants, and training students.

Kalamazoo, Michigan, United States

Cloned, expressed, and purified NSP3 RNA binding domain (RBD) constructs to study binding and complex assembly. RBD contained distinctly structured subdomains: N-terminal, helix 5, and C-terminal subdomains. I Utilized bioinformatics and modeling to determine subdomains and EMSA experiments to investigate RNA-binding. The second project was to study the nucleic acid binding of the PWI domain-containing proteins. The PWI domain contains conserved Proline (P)-Tryptophan (W)-Isoleucine (I) tripeptide sequence (motif). The PWI domain comprises the PWI motif and a positively charged region. Cloned, expressed, and purified canonical PWI motif-containing proteins involved in pre-mRNA processing, the pre-mRNA processing protein 3 (Prp3), RNA-binding motif protein 25 (RBM25), and SR-related nuclear matrix protein (SRm160) to study nucleic acid binding. Mutagenesis confirmed that the surface's hydrophobic and hydrophilic amino acids altered protein solubility. I assigned the backbone of PRP3(1-112) using a classic triple resonance approach, which involved HNCACB, CBCACONH, HNCA, HNCOCA, HNCO, 1H- 15N NOESY, HNHA, and HBHACONH experiments. I also collected T1, T2, and steady-state heteronuclear NOE nitrogen relaxation experiments and analyzed them using a three-parameter exponential least-square fit. The results showed that the N-terminal ~75 amino acid residues of the PRP3(1-112) protein construct are structured. In contrast, the C terminal residues were dynamic.The PWI domains from PRP3, SRm160, and RBM25 bind nucleic acids with a low micromolar binding affinity, and two or more proteins were involved in complex formation. NMR spectroscopy revealed the structural and conformationally dynamic properties of the domain.Mentored students on best laboratory practices and set up proper molecular and biochemical experiments. Guided students to achieve a well-thought-out and focused research objective. Taught general, organic chemistry, and biochemistry lab.

Nairobi, Kenya

Taught and graded physical and organic chemistry labs, graded laboratory reports, and guided undergraduates in the research lab.

Nairobi, Kenya

Marketed medicines to medical practitioners and collected orders to achieve sales targets. Launched new medical products and expanded existing product markets, leading to millions in sales orders and significantly improving my communication, creativity, interpersonal, and persuasive skills.

Doctor Of Philosophy - Phd, Chemistry

Structural Biology | Biochemistry | NMR Spectroscopy | Biophysical Chemistry

Master Of Science (Msc), Chemistry

Surface Chemistry | Physical Chemistry | Adsorption Studies