Sandbox GGC12

Human serum albumin or HSA is one of the major types of proteins that are present in the plasma composition. It is such abundant that its concentration on a common blood sample is 5 grams per 100 milliliters. Due to its high concentration in plasma as well as its physiological and pharmaceutical features, it has been subjected to several studies to determine its 3D structure, function, domains, important binding sites, and diseases. The primary structure of HSA describes a single polypeptide with 585 amino acids with the characteristics of having 17 pairs of disulfide bridges, one free cysteine ^[1]. It has been discovered that there are highly conserved sequences between bovine, human and rat albumins such as Trp-212, 143-155 and 244-263 sequence ^[2]. It is composed of three domains at positions 19-210, 211-403, and 404-601 with two subdomains each (Ia&b, IIa&b, and IIIa&b). The subcellular location of these protein is the extracellular region on the outside of the cell membrane or secreted. There are 11 metal binding sites, including 1 copper site, 7 calcium sites, 3 zinc sites, additionally, 1 binding site for bilirubin and 1 site for aspirin-acetylated lysine ^[3].

Function

HSA functions as the essential protein for the circulatory system, however, it has been discovered that possesses a high affinity an extensive range of amino acids, ligands, fatty acids, metals like copper and zinc, and metabolites such as bilirubin and drugs ingredients ^[4].Its fundamental role is to transport these varied types of solutes through the bloodstream to specific organs, control the level of pH and osmotic pressure of the plasma, and interaction with the cell membrane exchange of molecules at binding sites ^[5]. It is considered to be the vital carrier of zinc in the plasma as well as the calcium and magnesium. In terms of affinity, the order from higher to lower affinity follows this pattern: zinc, calcium and magnesium ^[6]. Pharmaceutically, it has been used to target certain organs with some drugs by HSA being the carrier. By performing experiments on E.coli, it was discovered that it inhibits enterobactin-mediated iron absorption from ferric transferrin due to its binding to the bacterial siderophore limiting the uptake of iron, and consequently, blocking the growth of E.coli ^[7].

Disease

Relevance

The relevance of this protein, HSA, relies on the its capacity to transports molecules through out the bloodstream. It helps move substances such as metals, amino acids, drugs, fatty acids to every part of the body because it is a protein present in the blood that flows around the body. It is a significant protein because it allows us to use it pharmaceutically to target certain organs with specific drugs. Additionally, it is essential for the control of the levels of pH and the osmotic pressure in the plasma. And finally, it is a protein that allows the cell membrane interact with the outer space of the cell by the help of HSA in the targeting of binding sites.

Structural highlights

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