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Arch Biochem Biophys. 2017 Dec 15;636:71-78. doi: 10.1016/j.abb.2017.11.001. Epub 2017 Nov 6.

Physiological serum copper concentrations found in malignancies cause unfolding induced aggregation of human serum albumin in vitro.

Author information

1
Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh, 202 002, India.
2
Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh, 202 002, India. Electronic address: imrananaseem2009@gmail.com.

Abstract

Malignancies are characterized by several drastic metabolic changes, one of which is a progressive rise in the levels of serum copper. This rise in serum copper is documented across all malignancies and across malignancies in several species. This study aims to explore in vitro the effect of increased copper levels on the structure of the blood protein human serum albumin. Exposure of human serum albumin to physiologically relevant copper concentrations for 21 days resulted in structural modifications in the protein which were evident by changes in the intrinsic florescence. A loss of the predominantly alpha helical structure of human serum albumin was recorded along with a tendency to form protein aggregates. This aggregation was characterized by Thioflavin T and Congo Red assays. Rayleigh light scattering and turbidity assays confirmed aggregation. The aggregates were visually confirmed using transmission electron microscopy. This is the first report implicating increased copper levels as a cause of aggregation of blood proteins in malignancies. The physiological and biochemical implications of this phenomenon are discussed.

KEYWORDS:

Aggregation; Cancer; Copper; Human serum albumin; Protein

PMID:
29122590
DOI:
10.1016/j.abb.2017.11.001
[Indexed for MEDLINE]

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