Abstract
Human carbonic anhydrases (hCAs) belong to a well characterized group of metalloenzymes that catalyze the conversion of carbonic dioxide into bicarbonate. There are currently 15 known human isoforms of carbonic anhydrase with different functions and distribution in the body. This links to the relevance of hCA variants to several diseases such as glaucoma, epilepsy, mountain sickness, ulcers, osteoporosis, obesity and cancer. This review will focus on two of the human isoforms, hCA I and hCA II. Both are cytosolic enzymes with similar topology and 60% sequence homology but different catalytic efficiency and stability. Proteins in general adsorb on surfaces and this is also the case for hCA I and hCA II. The adsorption process can lead to alteration of the original function of the protein. However, if the function is preserved interesting biotechnological applications can be developed. This review will cover the knowledge about the interaction between hCAs and nanomaterials. We will highlight how the interaction may lead to conformational changes that render the enzyme inactive. Moreover, the importance of different factors on the final effect on hCAs, such as protein stability, protein hydrophobic or charged patches and chemistry of the nanoparticle surface will be discussed.
Highlights
Carbonic anhydrases (CAs) are found in species from all kingdoms and are categorized into eight distinct classes (α, β, γ, δ, ζ, η, θ, and ζ) [1,2]
The outcome of if a protein is mixed with a nanoparticle will depend on which protein it is and the material, size, shape and surface modification of the nanoparticle
We have summarized the knowledge gained so far on the interaction from one of the more studied proteins, Human carbonic anhydrases (hCAs) I and II, and model nanoparticles, silica and polystyrene
Summary
Carbonic anhydrases (CAs) are found in species from all kingdoms and are categorized into eight distinct classes (α, β, γ, δ, ζ, η, θ, and ζ) [1,2]. CAs in mammals are involved in many physiological and pathological processes such as respiration and CO2 transport, pH and CO2 homeostasis, biosynthetic reactions, calcification and tumor progression between others (more comprehensive information on physiological functions and pathogenicity can be found in diverse reviews) [4,5,6]. Due to this variety of functions, CAs are a potential target for therapeutic drugs in the treatment of diseases such as glaucoma, epilepsy, mountain sickness, ulcers, osteoporosis, obesity and cancer [4,5]. This review will focus on two cytosolic CAs from the α-class, human carbonic anhydrase I and II (hCA I and hCA II) and their interaction with nanomaterials of diverse chemistry and size. We highlight what has been learned regarding the interaction between NPs and one of the hitherto most thoroughly characterized model proteins
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