Scholars@Duke
Kathryn Haas

Kathryn Haas

Associate Professor of the Practice of Chemistry
Chemistry
Box 90346, Durham, NC 27708-0346
1224 French Science Center, 124 Science Drive Box 90346, Durham, NC 27708
Office hours

Scholarly Works - Journal articles

Cu(I) and Cu(II) binding by hyperactive variants of the human CTR1 N-terminus: Insights from cellular and model peptide studies.

Journal article Journal of inorganic biochemistry · September 2026 Featured Publication Copper (Cu) trafficking requires precise control of Cu(II)/Cu(I) redox chemistry to enable cellular acquisition while preventing toxicity. Human Cu transporter 1 protein (hCTR1) mediates cellular Cu uptake, yet key molecular details governing its extracell ... Full text Open Access Cite

Investigating Cu(I) binding to model peptides of N-terminal Aβ isoforms.

Journal article Journal of inorganic biochemistry · April 2024 Amyloid beta (Aβ) peptides and copper (Cu) ions are each involved in critical biological processes including antimicrobial activity, regulation of synaptic function, angiogenesis, and others. Aβ binds to Cu and may play a role in Cu trafficking. Aβ peptide ... Full text Cite

How did STEM students respond to a cross-campus discussion forum about macroethics? An exploratory content analysis of students’ written reflections

Journal article SN Social Sciences · September 1, 2023 Ethics education is increasingly recognized as an essential element of undergraduate programs focused on science, technology, engineering, and mathematics (STEM). One method is training future STEM professionals in responsible conduct of research at the in ... Full text Cite

Exploration of the Potential Role of Serum Albumin in the Delivery of Cu(I) to Ctr1.

Journal article Inorganic chemistry · March 2023 Human serum albumin (HSA) is the major copper (Cu) carrier in blood. The majority of previous studies that have investigated Cu interactions with HSA have focused primarily on the Cu(II) oxidation state. Yet, cellular Cu uptake by the human copper transpor ... Full text Cite

Exploration of the Potential Role for Aβ in Delivery of Extracellular Copper to Ctr1.

Journal article Inorganic chemistry · December 2020 Featured Publication Amyloid beta (Aβ) peptides are notorious for their involvement in Alzheimer's disease (AD), by virtue of their propensity to aggregate to form oligomers, fibrils, and eventually plaques in the brain. Nevertheless, they appear to be essential for correct ne ... Full text Cite

Using N-Terminal Coordination of Cu(II) and Ni(II) to Isolate the Coordination Environment of Cu(I) and Cu(II) Bound to His13 and His14 in Amyloid-β(4-16).

Journal article Inorganic chemistry · November 2019 Featured Publication The amyloid-β (Aβ) peptide is a cleavage product of the amyloid precursor protein and has been implicated as a central player in Alzheimer's disease. The N-terminal end of Aβ is variable, and different proportions of these variable-length Aβ peptides are p ... Full text Cite

The N-terminal 14-mer model peptide of human Ctr1 can collect Cu(ii) from albumin. Implications for copper uptake by Ctr1.

Journal article Metallomics : integrated biometal science · December 2018 Featured Publication Human cells acquire copper primarily via the copper transporter 1 protein, hCtr1. We demonstrate that at extracellular pH 7.4 CuII is bound to the model peptide hCtr11-14via an ATCUN motif and such complexes are strong enough to collect CuII from albumin, ... Full text Cite

Collaborating with Undergraduates To Contribute to Biochemistry Community Resources.

Journal article Biochemistry · January 2018 Featured Publication Course-based undergraduate research experiences (CUREs) have gained traction as effective ways to expand the impact of undergraduate research while fulfilling pedagogical goals. In this Perspective, we present innovative ways to incorporate fundamental ben ... Full text Cite

Structure and Affinity of Cu(I) Bound to Human Serum Albumin.

Journal article Inorganic chemistry · December 2017 Featured Publication Human serum albumin (HSA) is a major Cu carrier in human blood and in cerebrospinal fluid. A major assumption is that Cu bound to HSA is in the Cu(II) oxidation state; thus, interactions between HSA and Cu(II) have been intensely investigated for over four ... Full text Cite

Specific Histidine Residues Confer Histatin Peptides with Copper-Dependent Activity against Candida albicans

Journal article Biochemistry · August 1, 2017 The histidine-rich salivary peptides of the histatin family are known to bind copper (Cu) and other metal ions in vitro; however, the details of these interactions are poorly understood, and their implications for in vivo antifungal activity have not been ... Full text Open Access Link to item Cite

Sequence proximity between Cu(II) and Cu(I) binding sites of human copper transporter 1 model peptides defines reactivity with ascorbate and O2.

Journal article Journal of inorganic biochemistry · May 2016 The critical nature of the copper transporter 1 (Ctr1) in human health has spurred investigation of Ctr1 structure and function. Ctr1 specifically transports Cu(I), the reduced form of copper, across the plasma membrane. Thus, extracellular Cu(II) must be ... Full text Open Access Cite

Model Peptide Studies Reveal a Mixed Histidine-Methionine Cu(I) Binding Site at the N-Terminus of Human Copper Transporter 1.

Journal article Inorganic chemistry · September 2015 Featured Publication Copper is a vital metal cofactor in enzymes that are essential to myriad biological processes. Cellular acquisition of copper is primarily accomplished through the Ctr family of plasma membrane copper transport proteins. Model peptide studies indicate that ... Full text Cite

Role of MTL-1, MTL-2, and CDR-1 in mediating cadmium sensitivity in Caenorhabditis elegans.

Journal article Toxicological sciences : an official journal of the Society of Toxicology · August 2012 Cadmium is an environmental toxicant whose exposure is associated with multiple human pathologies. To prevent cadmium-induced toxicity, organisms produce a variety of detoxification molecules. In response to cadmium, the nematode Caenorhabditis elegans inc ... Full text Cite

Model peptides provide new insights into the role of histidine residues as potential ligands in human cellular copper acquisition via Ctr1.

Journal article Journal of the American Chemical Society · March 2011 Cellular acquisition of copper in eukaryotes is primarily accomplished through the Ctr family of copper transport proteins. In both humans and yeast, methionine-rich "Mets" motifs in the amino-terminal extracellular domain of Ctr1 are thought to be respons ... Full text Cite

Development of next-generation photolabile copper cages with improved copper binding properties.

Journal article Dalton transactions (Cambridge, England : 2003) · October 2010 Seven new nitrogen-donor ligands that contain a photoactive nitrophenyl group within the ligand backbone have been prepared and evaluated for their binding affinity for copper(ii) and zinc(ii). Among this series, the ligand 3Gcage (pyridine-2-carboxylic ac ... Full text Open Access Cite

A photo-caged platinum(II) complex that increases cytotoxicity upon light activation

Journal article European Journal of Inorganic Chemistry · January 1, 2010 A novel platinum(II) photocaged complex called [Pt(cage)] has been prepared and characterized by X-ray crystallography. The complex contains a photolabile nitrophenyl group incorporated into the backbone of a tetradentate ligand that contains two pyridyl a ... Full text Cite

A photolabile ligand for light-activated release of caged copper.

Journal article Journal of the American Chemical Society · September 2008 A photosensitive caged copper complex has been prepared from a tetradentate ligand (H2cage) composed of two pyridyl-amide arms connected by a photoreactive nitrophenyl group. H2cage binds Cu2+ in aqueous solution with a stability constant (log beta) of 10. ... Full text Cite