Principles and practice of determining metal–protein affinities

Young, Tessa R.; Xiao, Zhiguang

doi:10.1042/bcj20200838

Cited by 31 publications

(30 citation statements)

References 106 publications

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“…Although the principles that describe metal formation in organisms are outside the scope of this review, we take the liberty to recommend readers to obtain corresponding details from other recently published review papers, where such phenomena as metal-biomolecule affinities [ 296 , 297 , 298 , 299 , 300 , 301 ], metal-ion binding sites based on amino acid sequences, and cellular dynamics of metal ion-exchange have been excellently represented. Moreover, recent advances in the understanding of mechanisms of metal formation in diverse biological systems are to be found in numerous overviews on metallomics.…”

Section: Discussionmentioning

confidence: 99%

Forced Biomineralization: A Review

2021

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Biologically induced and controlled mineralization of metals promotes the development of protective structures to shield cells from thermal, chemical, and ultraviolet stresses. Metal biomineralization is widely considered to have been relevant for the survival of life in the environmental conditions of ancient terrestrial oceans. Similar behavior is seen among extremophilic biomineralizers today, which have evolved to inhabit a variety of industrial aqueous environments with elevated metal concentrations. As an example of extreme biomineralization, we introduce the category of “forced biomineralization”, which we use to refer to the biologically mediated sequestration of dissolved metals and metalloids into minerals. We discuss forced mineralization as it is known to be carried out by a variety of organisms, including polyextremophiles in a range of psychrophilic, thermophilic, anaerobic, alkaliphilic, acidophilic, and halophilic conditions, as well as in environments with very high or toxic metal ion concentrations. While much additional work lies ahead to characterize the various pathways by which these biominerals form, forced biomineralization has been shown to provide insights for the progression of extreme biomimetics, allowing for promising new forays into creating the next generation of composites using organic-templating approaches under biologically extreme laboratory conditions relevant to a wide range of industrial conditions.

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Section: Discussionmentioning

confidence: 99%

Forced Biomineralization: A Review

2021

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“…The important aspect of metal ions’ impacts on the human body are metal-mediated protein–protein interactions. Understanding these interactions is central to understanding the molecular details of heavy-metal impact on human health [ 95 ].…”

Section: The Impact Of Toxic Metals On Human Enzymatic Pathwaysmentioning

confidence: 99%

Heavy Metals and Human Health: Possible Exposure Pathways and the Competition for Protein Binding Sites

2021

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Heavy metals enter the human body through the gastrointestinal tract, skin, or via inhalation. Toxic metals have proven to be a major threat to human health, mostly because of their ability to cause membrane and DNA damage, and to perturb protein function and enzyme activity. These metals disturb native proteins’ functions by binding to free thiols or other functional groups, catalyzing the oxidation of amino acid side chains, perturbing protein folding, and/or displacing essential metal ions in enzymes. The review shows the physiological and biochemical effects of selected toxic metals interactions with proteins and enzymes. As environmental contamination by heavy metals is one of the most significant global problems, some detoxification strategies are also mentioned.

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“…ITC can underestimate metal binding affinities due to lack of sensitivity, lack of specificity, and potential side reactions (e.g. competition with buffers) [48]. Thus, the Zn affinities of AdcAI were reexamined here by competition with the colorimetric Zn indicator Mag-fura2 (Mf2).…”

Section: Molecular Basis For the Action Of Hst5 In Weakly Influencing Zn Availabilitymentioning

confidence: 99%

The role of metal binding in the function of the human salivary antimicrobial peptide histatin-5

Stewart

Hong

Holmes

et al. 2022

Preprint

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The family of human salivary histidine-rich peptides known as histatins bind zinc (Zn) and copper (Cu), but whether they contribute to nutritional immunity by influencing Zn and/or Cu availability has not been examined. We hypothesised that histatin-5 (Hst5) limits Zn availability (and promotes bacterial Zn starvation) and/or raises Cu availability (and promotes bacterial Cu poisoning). To test this hypothesis, Group A Streptococcus (GAS), which colonises the human oropharynx, was used as a model bacterium. Contrary to our hypothesis, Hst5 did not strongly influence Zn availability. This peptide did not induce expression of Zn uptake genes in GAS, nor did it suppress growth of an ΔadcAI mutant strain that is impaired in Zn uptake. Equilibrium competition measurements confirmed that Hst5 binds Zn weakly and does not compete with the high-affinity Zn uptake protein AdcAI for binding Zn. By contrast, Hst5 bound Cu with a high affinity and strongly influenced Cu availability. However, contrary to our hypothesis, Hst5 did not promote Cu toxicity. Instead, this peptide suppressed expression of Cu-inducible genes in GAS, stopped intracellular accumulation of Cu, and rescued growth of a ΔcopA mutant strain that is impaired in Cu efflux in the presence of added Cu. These findings led us to propose a new role for Hst5 and salivary histatins as major Cu buffers in saliva that reduce the potential negative effects of Cu exposure to microbes. We speculate that histatins promote oral and oropharyngeal health by contributing to microbial homeostasis in these host niches.

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Principles and practice of determining metal–protein affinities

Cited by 31 publications

References 106 publications

Forced Biomineralization: A Review

Forced Biomineralization: A Review

Heavy Metals and Human Health: Possible Exposure Pathways and the Competition for Protein Binding Sites

The role of metal binding in the function of the human salivary antimicrobial peptide histatin-5

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